Thrombin
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Aliases | F2, PT, RPRGL2, THPH1, coagulation factor II, thrombin | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 176930; MGI: 88380; HomoloGene: 426; GeneCards: F2; OMA:F2 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Prothrombin (Coagulation factor II) is encoded in the human by the F2 gene. It is proteolytically cleaved during the clotting process by the prothrombinase enzyme complex to form thrombin.
Thrombin (Factor IIa) (EC 3.4.21.5, fibrinogenase, thrombase, thrombofort, topical, thrombin-C, tropostasin, activated blood-coagulation factor II, E thrombin, beta-thrombin, gamma-thrombin) is a serine protease, that converts fibrinogen into strands of insoluble fibrin, as well as catalyzing many other coagulation-related reactions.[5][6]
History
After the description of fibrinogen and fibrin, Alexander Schmidt hypothesised the existence of an enzyme that converts fibrinogen into fibrin in 1872.[7]
Prothrombin was discovered by Pekelharing in 1894.[8][9][10]
Physiology
Synthesis
Thrombin is produced by the enzymatic cleavage of two sites on prothrombin by activated Factor X (Xa). The activity of factor Xa is greatly enhanced by binding to activated Factor V (Va), termed the prothrombinase complex. Prothrombin is produced in the liver and is co-translationally modified in a vitamin K-dependent reaction that converts 10-12 glutamic acids in the N terminus of the molecule to gamma-carboxyglutamic acid (Gla).[11] In the presence of calcium, the Gla residues promote the binding of prothrombin to phospholipid bilayers. Deficiency of vitamin K or administration of the anticoagulant warfarin inhibits the production of gamma-carboxyglutamic acid residues, slowing the activation of the coagulation cascade.
In human adults, the normal blood level of antithrombin activity has been measured to be around 1.1 units/mL. Newborn levels of thrombin steadily increase after birth to reach normal adult levels, from a level of around 0.5 units/mL 1 day after birth, to a level of around 0.9 units/mL after 6 months of life.[12]
Mechanism of action
In the blood coagulation pathway, thrombin acts to convert factor XI to XIa, VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa. In the conversion of fibrinogen into fibrin, thrombin catalyzes the cleavage of fibrinopeptides A and B from the respective Aα and Bβ chains of fibrinogen to form fibrin monomers.[13]
Factor XIIIa is a transglutaminase that catalyzes the formation of covalent bonds between lysine and glutamine residues in fibrin. The covalent bonds increase the stability of the fibrin clot. Thrombin interacts with thrombomodulin.[14][15]
As part of its activity in the coagulation cascade, thrombin also promotes platelet activation and aggregation via activation of protease-activated receptors on the cell membrane of the platelet.
Negative feedback
Thrombin bound to thrombomodulin activates protein C, an inhibitor of the coagulation cascade. The activation of protein C is greatly enhanced following the binding of thrombin to thrombomodulin, an integral membrane protein expressed by endothelial cells. Activated protein C inactivates factors Va and VIIIa. Binding of activated protein C to protein S leads to a modest increase in its activity. Thrombin is also inactivated by antithrombin, a serine protease inhibitor.
Structure
The molecular weight of prothrombin is approximately 72,000 Da. The catalytic domain is released from prothrombin fragment 1.2 to create the active enzyme thrombin, which has a molecular weight of 36,000 Da. Structurally, it is a member of the large PA clan of proteases.
Prothrombin is composed of four domains; an N-terminal Gla domain, two kringle domains and a C-terminal trypsin-like serine protease domain. Factor Xa with factor V as a cofactor leads to cleavage of the Gla and two Kringle domains (forming together a fragment called fragment 1.2) and leave thrombin, consisting solely of the serine protease domain.[17]
As is the case for all serine proteases, prothrombin is converted to active thrombin by proteolysis of an internal peptide bond, exposing a new N-terminal Ile-NH3. The historic model of activation of serine proteases involves insertion of this newly formed N-terminus of the heavy chain into the β-barrel promoting the correct conformation of the catalytic residues.[18] Contrary to crystal structures of active thrombin, hydrogen-deuterium exchange mass spectrometry studies indicate that this N-terminal Ile-NH3 does not become inserted into the β-barrel in the apo form of thrombin. However, binding of the active fragment of thrombomodulin appears to allosterically promote the active conformation of thrombin by inserting this N-terminal region.[19]
Gene
There are an estimated 30 people in the world that have been diagnosed with the congenital form of Factor II deficiency,[20] which should not be confused with the prothrombin G20210A mutation, which is also called the factor II mutation. Prothrombin G20210A is congenital.[21]
Prothrombin G20210A is not usually accompanied by other factor mutations (i.e., the most common is factor V Leiden). The gene may be inherited heterozygous (1 pair), or much more rarely, homozygous (2 pairs), and is not related to gender or blood type. Homozygous mutations increase the risk of thrombosis more than heterozygous mutations, but the relative increased risk is not well documented. Other potential risks for thrombosis, such as oral contraceptives may be additive. The previously reported relationship of inflammatory bowel disease (i.e., Crohn's disease or ulcerative colitis) and prothrombin G20210A or factor V Leiden mutation have been contradicted by research.[22]
Role in disease
Activation of prothrombin is crucial in physiological and pathological coagulation. Various rare diseases involving prothrombin have been described (e.g., hypoprothrombinemia). Anti-prothrombin antibodies in autoimmune disease may be a factor in the formation of the lupus anticoagulant (also known as antiphospholipid syndrome). Hyperprothrombinemia can be caused by the G20210A mutation.
Thrombin, a potent vasoconstrictor and mitogen, is implicated as a major factor in vasospasm following subarachnoid hemorrhage. Blood from a ruptured cerebral aneurysm clots around a cerebral artery, releasing thrombin. This can induce an acute and prolonged narrowing of the blood vessel, potentially resulting in cerebral ischemia and infarction (stroke).
Beyond its key role in the dynamic process of thrombus formation, thrombin has a pronounced pro-inflammatory character, which may influence the onset and progression of atherosclerosis. Acting via its specific cell membrane receptors (protease activated receptors: PAR-1, PAR-3 and PAR-4), which are abundantly expressed in all arterial vessel wall constituents, thrombin has the potential to exert pro-atherogenic actions such as inflammation, leukocyte recruitment into the atherosclerotic plaque, enhanced oxidative stress, migration and proliferation of vascular smooth muscle cells, apoptosis and angiogenesis.[23][24][25]
Thrombin is implicated in the physiology of blood clots. Its presence indicates the existence of a clot. In 2013 a system for detecting the presence of thrombin was developed in mice. It combines peptide-coated iron oxide attached to "reporter chemicals". When a peptide binds to a thrombin molecule, the report is released and appears in the urine where it can be detected. Human testing has not been conducted.[26]
Applications
Research tool
Due to its high proteolytic specificity, thrombin is a valuable biochemical tool. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is commonly included in linker regions of recombinant fusion protein constructs. Following purification of the fusion protein, thrombin can be used to selectively cleave between the arginine and glycine residues of the cleavage site, effectively removing the purification tag from the protein of interest with a high degree of specificity.
Medicine and surgery
Prothrombin complex concentrate and fresh frozen plasma are prothrombin-rich coagulation factor preparations that can be used to correct deficiencies (usually due to medication) of prothrombin. Indications include intractable bleeding due to warfarin.
Manipulation of prothrombin is central to the mode of action of most anticoagulants. Warfarin and related drugs inhibit vitamin K-dependent carboxylation of several coagulation factors, including prothrombin. Heparin increases the affinity of antithrombin to thrombin (as well as factor Xa). The direct thrombin inhibitors, a newer class of medication, directly inhibit thrombin by binding to its active site.
Recombinant thrombin is available as a powder for reconstitution into aqueous solution. It can be applied topically during surgery, as an aid to hemostasis. It can be useful for controlling minor bleeding from capillaries and small venules, but ineffective and not indicated for massive or brisk arterial bleeding.[27][28][29]
Food production
Thrombin, combined with fibrinogen, is sold under the brand name Fibrimex for use as a binding agent for meat. Both proteins in Fibrimex derives from porcine or bovine blood.[30] According to the manufacturer it can be used to produce new kinds of mixed meats (for example combining beef and fish seamlessly). The manufacturer also states that it can be used to combine whole muscle meat, form and portion these, thus cutting down on production costs without a loss in quality.[31]
General secretary Jan Bertoft of Swedish Consumers' Association has stated that "there is danger of misleading the consumers since there is no way to tell this reconstituted meat from real meat".[30]
See also
- Cerastocytin
- Fibrin glue
- Fibrinogen
- PA clan of proteases
- The Proteolysis Map
- Thrombin generation assay
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000180210 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027249 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Royle NJ, Irwin DM, Koschinsky ML, MacGillivray RT, Hamerton JL (May 1987). "Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively". Somatic Cell and Molecular Genetics. 13 (3): 285–92. doi:10.1007/BF01535211. PMID 3474786. S2CID 45686258.
- ^ Degen SJ, Davie EW (September 1987). "Nucleotide sequence of the gene for human prothrombin". Biochemistry. 26 (19): 6165–77. doi:10.1021/bi00393a033. PMID 2825773.
- ^ Schmidt A (1872). "Neue Untersuchungen ueber die Fasserstoffesgerinnung". Pflügers Archiv für die gesamte Physiologie. 6: 413–538. doi:10.1007/BF01612263. S2CID 37273997.
- ^ Kaushansky K, Lichtman M, Prchal J, Levi M, Press O, Burns L, Caligiuri M (2015). Williams Hematology. McGraw-Hill. p. 1918. ISBN 9780071833011.
- ^ Quick AJ (1957). Hemorrhagic Diseases. Philadelphia: Lea and Febiger. pp. 451–490. OCLC 599096191.
- ^ Morawitz P (1905). "Die Chemie der Blutgerinnung". Ergeb Physiol. 4: 307–422. doi:10.1007/BF02321003. S2CID 84003009.
- ^ Knorre DG, Kudryashova NV, Godovikova TS (October 2009). "Chemical and functional aspects of posttranslational modification of proteins". Acta Naturae. 1 (3): 29–51. doi:10.32607/20758251-2009-1-3-29-51. PMC 3347534. PMID 22649613.
- ^ Andrew M, Paes B, Milner R, Johnston M, Mitchell L, Tollefsen DM, Powers P (July 1987). "Development of the human coagulation system in the full-term infant". Blood. 70 (1): 165–72. doi:10.1182/blood.V70.1.165.165. PMID 3593964.
- ^ Wolberg AS (September 2012). "Determinants of fibrin formation, structure, and function". Curr Opin Hematol. 19 (5): 349–56. doi:10.1097/MOH.0b013e32835673c2. PMID 22759629. S2CID 11358104.
- ^ Bajzar L, Morser J, Nesheim M (July 1996). "TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex". The Journal of Biological Chemistry. 271 (28): 16603–8. doi:10.1074/jbc.271.28.16603. PMID 8663147.
- ^ Jakubowski HV, Owen WG (July 1989). "Macromolecular specificity determinants on thrombin for fibrinogen and thrombomodulin". The Journal of Biological Chemistry. 264 (19): 11117–21. doi:10.1016/S0021-9258(18)60437-5. PMID 2544585.
- ^ PDB: 1nl2; Huang M, Rigby AC, Morelli X, Grant MA, Huang G, Furie B, Seaton B, Furie BC (September 2003). "Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins". Nature Structural Biology. 10 (9): 751–6. doi:10.1038/nsb971. PMID 12923575. S2CID 7751100.
- ^ Davie EW, Kulman JD (April 2006). "An overview of the structure and function of thrombin". Seminars in Thrombosis and Hemostasis. 32 (Suppl 1): 3–15. doi:10.1055/s-2006-939550. PMID 16673262. S2CID 36616995.
- ^ Huber R, Bode W (1978-03-01). "Structural basis of the activation and action of trypsin". Accounts of Chemical Research. 11 (3): 114–122. doi:10.1021/ar50123a006. ISSN 0001-4842.
- ^ Handley LD, Treuheit NA, Venkatesh VJ, Komives EA (November 2015). "Thrombomodulin Binding Selects the Catalytically Active Form of Thrombin". Biochemistry. 54 (43): 6650–8. doi:10.1021/acs.biochem.5b00825. PMC 4697735. PMID 26468766.
- ^ Degen SJ, McDowell SA, Sparks LM, Scharrer I (February 1995). "Prothrombin Frankfurt: a dysfunctional prothrombin characterized by substitution of Glu-466 by Ala". Thrombosis and Haemostasis. 73 (2): 203–9. doi:10.1055/s-0038-1653751. PMID 7792730. S2CID 20144699.
- ^ Varga EA, Moll S (July 2004). "Cardiology patient pages. Prothrombin 20210 mutation (factor II mutation)". Circulation. 110 (3): e15–8. doi:10.1161/01.CIR.0000135582.53444.87. PMID 15262854.
- ^ Bernstein CN, Sargent M, Vos HL, Rosendaal FR (February 2007). "Mutations in clotting factors and inflammatory bowel disease". The American Journal of Gastroenterology. 102 (2): 338–43. doi:10.1111/j.1572-0241.2006.00974.x. PMID 17156138. S2CID 19895315.
- ^ Borissoff JI, Spronk HM, Heeneman S, ten Cate H (June 2009). "Is thrombin a key player in the 'coagulation-atherogenesis' maze?". Cardiovascular Research. 82 (3): 392–403. doi:10.1093/cvr/cvp066. PMID 19228706.
- ^ Borissoff JI, Heeneman S, Kilinç E, Kassák P, Van Oerle R, Winckers K, Govers-Riemslag JW, Hamulyák K, Hackeng TM, Daemen MJ, ten Cate H, Spronk HM (August 2010). "Early atherosclerosis exhibits an enhanced procoagulant state". Circulation. 122 (8): 821–30. doi:10.1161/CIRCULATIONAHA.109.907121. PMID 20697022.
- ^ Borissoff JI, Spronk HM, ten Cate H (May 2011). "The hemostatic system as a modulator of atherosclerosis". The New England Journal of Medicine. 364 (18): 1746–60. doi:10.1056/NEJMra1011670. PMID 21542745.
- ^ Economist (2013-11-05). "Nanomedicine: Particle physiology". The Economist. Retrieved 2013-12-15.
- ^ Chapman WC, Singla N, Genyk Y, McNeil JW, Renkens KL, Reynolds TC, Murphy A, Weaver FA (August 2007). "A phase 3, randomized, double-blind comparative study of the efficacy and safety of topical recombinant human thrombin and bovine thrombin in surgical hemostasis". Journal of the American College of Surgeons. 205 (2): 256–65. doi:10.1016/j.jamcollsurg.2007.03.020. PMID 17660072.
- ^ Singla NK, Ballard JL, Moneta G, Randleman CD, Renkens KL, Alexander WA (July 2009). "A phase 3b, open-label, single-group immunogenicity and safety study of topical recombinant thrombin in surgical hemostasis". Journal of the American College of Surgeons. 209 (1): 68–74. doi:10.1016/j.jamcollsurg.2009.03.016. PMID 19651065.
- ^ Greenhalgh DG, Gamelli RL, Collins J, Sood R, Mozingo DW, Gray TE, Alexander WA (2009). "Recombinant thrombin: safety and immunogenicity in burn wound excision and grafting". Journal of Burn Care & Research. 30 (3): 371–9. doi:10.1097/BCR.0b013e3181a28979. PMID 19349898. S2CID 3678462.
- ^ a b "Sverige röstade ja till köttklister" [Sweden voted in favor of the meat paste] (in Swedish). Dagens Nyheter. 2010-02-09. Retrieved 2010-10-17.
- ^ "Welcome to Fibrimex". Fibrimex website. Sonac. Retrieved 2019-02-28.
Further reading
- Esmon CT (July 1995). "Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface". FASEB Journal. 9 (10): 946–55. doi:10.1096/fasebj.9.10.7615164. PMID 7615164. S2CID 19565674.
- Wu H, Zhang Z, Li Y, Zhao R, Li H, Song Y, Qi J, Wang J (October 2010). "Time course of upregulation of inflammatory mediators in the hemorrhagic brain in rats: correlation with brain edema". Neurochemistry International. 57 (3): 248–53. doi:10.1016/j.neuint.2010.06.002. PMC 2910823. PMID 20541575.
- Lenting PJ, van Mourik JA, Mertens K (December 1998). "The life cycle of coagulation factor VIII in view of its structure and function". Blood. 92 (11): 3983–96. doi:10.1182/blood.V92.11.3983. PMID 9834200.
- Plow EF, Cierniewski CS, Xiao Z, Haas TA, Byzova TV (July 2001). "AlphaIIbbeta3 and its antagonism at the new millennium". Thrombosis and Haemostasis. 86 (1): 34–40. doi:10.1055/s-0037-1616198. PMID 11487023. S2CID 74389210.
- Maragoudakis ME, Tsopanoglou NE, Andriopoulou P (April 2002). "Mechanism of thrombin-induced angiogenesis". Biochemical Society Transactions. 30 (2): 173–7. doi:10.1042/BST0300173. PMID 12023846.
- Howell DC, Laurent GJ, Chambers RC (April 2002). "Role of thrombin and its major cellular receptor, protease-activated receptor-1, in pulmonary fibrosis". Biochemical Society Transactions. 30 (2): 211–6. doi:10.1042/BST0300211. PMID 12023853. S2CID 32822567.
- Firth SM, Baxter RC (December 2002). "Cellular actions of the insulin-like growth factor binding proteins". Endocrine Reviews. 23 (6): 824–54. doi:10.1210/er.2001-0033. PMID 12466191.
- Minami T, Sugiyama A, Wu SQ, Abid R, Kodama T, Aird WC (January 2004). "Thrombin and phenotypic modulation of the endothelium". Arteriosclerosis, Thrombosis, and Vascular Biology. 24 (1): 41–53. doi:10.1161/01.ATV.0000099880.09014.7D. PMID 14551154.
- De Cristofaro R, De Candia E (June 2003). "Thrombin domains: structure, function and interaction with platelet receptors". Journal of Thrombosis and Thrombolysis. 15 (3): 151–63. doi:10.1023/B:THRO.0000011370.80989.7b. PMID 14739624.
- Tsopanoglou NE, Maragoudakis ME (February 2004). "Role of thrombin in angiogenesis and tumor progression". Seminars in Thrombosis and Hemostasis. 30 (1): 63–9. doi:10.1055/s-2004-822971. PMID 15034798. S2CID 260320933.
- Bode W (2007). "Structure and interaction modes of thrombin". Blood Cells, Molecules & Diseases. 36 (2): 122–30. doi:10.1016/j.bcmd.2005.12.027. PMID 16480903.
- Wolberg AS (May 2007). "Thrombin generation and fibrin clot structure". Blood Reviews. 21 (3): 131–42. doi:10.1016/j.blre.2006.11.001. PMID 17208341.
- Degen S (1995). "Prothrombin". In High K, Roberts H (eds.). Molecular Basis of Thrombosis and Hemostasis. Marcel Dekker. p. 75. ISBN 9780824795016.
External links
- The MEROPS online database for peptidases and their inhibitors: S01.217 Archived 2019-09-19 at the Wayback Machine
- Kujovich JL (February 2021). Adam MP, Ardinger HH, Pagon RA, et al. (eds.). "Prothrombin Thrombophilia". GeneReviews. Seattle WA: University of Washington, Seattle. PMID 20301327. NBK1148.
- Anti-coagulation & proteases on YouTube by The Proteolysis Map-animation
- [1] PMAP: The Proteolysis Map/Thrombin
- Thrombin: RCSB PDB Molecule of the Month Archived 2013-10-05 at the Wayback Machine
- Prothrombin Structure
- PDBe-KB provides an overview of all the structure information available in the PDB for Human Thrombin.
- PDBe-KB provides an overview of all the structure information available in the PDB for Mouse Thrombin.
- v
- t
- e
- 1a2c: STRUCTURE OF THROMBIN INHIBITED BY AERUGINOSIN298-A FROM A BLUE-GREEN ALGA
- 1a3b: COMPLEX OF HUMAN ALPHA-THROMBIN WITH THE BIFUNCTIONAL BORONATE INHIBITOR BOROLOG1
- 1a3e: COMPLEX OF HUMAN ALPHA-THROMBIN WITH THE BIFUNCTIONAL BORONATE INHIBITOR BOROLOG2
- 1a46: THROMBIN COMPLEXED WITH HIRUGEN AND A BETA-STRAND MIMETIC INHIBITOR
- 1a4w: CRYSTAL STRUCTURES OF THROMBIN WITH THIAZOLE-CONTAINING INHIBITORS: PROBES OF THE S1' BINDING SITE
- 1a5g: HUMAN THROMBIN COMPLEXED WITH NOVEL SYNTHETIC PEPTIDE MIMETIC INHIBITOR AND HIRUGEN
- 1a61: THROMBIN COMPLEXED WITH A BETA-MIMETIC THIAZOLE-CONTAINING INHIBITOR
- 1abi: STRUCTURE OF THE HIRULOG 3-THROMBIN COMPLEX AND NATURE OF THE S' SUBSITES OF SUBSTRATES AND INHIBITORS
- 1abj: STRUCTURE OF THE HIRULOG 3-THROMBIN COMPLEX AND NATURE OF THE S' SUBSITES OF SUBSTRATES AND INHIBITORS
- 1ad8: COMPLEX OF THROMBIN WITH AND INHIBITOR CONTAINING A NOVEL P1 MOIETY
- 1ae8: HUMAN ALPHA-THROMBIN INHIBITION BY EOC-D-PHE-PRO-AZALYS-ONP
- 1aht: CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN COMPLEXED WITH HIRUGEN AND P-AMIDINOPHENYLPYRUVATE) AT 1.6 ANGSTROMS RESOLUTION
- 1ai8: HUMAN ALPHA-THROMBIN TERNARY COMPLEX WITH THE EXOSITE INHIBITOR HIRUGEN AND ACTIVE SITE INHIBITOR PHCH2OCO-D-DPA-PRO-BOROMPG
- 1aix: HUMAN ALPHA-THROMBIN TERNARY COMPLEX WITH EXOSITE INHIBITOR HIRUGEN AND ACTIVE SITE INHIBITOR PHCH2OCO-D-DPA-PRO-BOROVAL
- 1awf: NOVEL COVALENT THROMBIN INHIBITOR FROM PLANT EXTRACT
- 1awh: NOVEL COVALENT THROMBIN INHIBITOR FROM PLANT EXTRACT
- 1ay6: THROMBIN INHIBITOR FROM THEONALLA, CYCLOTHEANAMIDE-BASED MACROCYCLIC TRIPEPTIDE MOTIF
- 1b5g: HUMAN THROMBIN COMPLEXED WITH NOVEL SYNTHETIC PEPTIDE MIMETIC INHIBITOR AND HIRUGEN
- 1b7x: STRUCTURE OF HUMAN ALPHA-THROMBIN Y225I MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE
- 1ba8: THROMBIN INHIBITOR WITH A RIGID TRIPEPTIDYL ALDEHYDES
- 1bb0: THROMBIN INHIBITORS WITH RIGID TRIPEPTIDYL ALDEHYDES
- 1bbr: THE STRUCTURE OF RESIDUES 7-16 OF THE A ALPHA CHAIN OF HUMAN FIBRINOGEN BOUND TO BOVINE THROMBIN AT 2.3 ANGSTROMS RESOLUTION
- 1bcu: ALPHA-THROMBIN COMPLEXED WITH HIRUGEN AND PROFLAVIN
- 1bhx: X-RAY STRUCTURE OF THE COMPLEX OF HUMAN ALPHA THROMBIN WITH THE INHIBITOR SDZ 229-357
- 1bth: STRUCTURE OF THROMBIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR
- 1c1u: RECRUITING ZINC TO MEDIATE POTENT, SPECIFIC INHIBITION OF SERINE PROTEASES
- 1c1v: RECRUITING ZINC TO MEDIATE POTENT, SPECIFIC INHIBITION OF SERINE PROTEASES
- 1c1w: RECRUITING ZINC TO MEDIATE POTENT, SPECIFIC INHIBITION OF SERINE PROTEASES
- 1c4u: SELECTIVE NON ELECTROPHILIC THROMBIN INHIBITORS WITH CYCLOHEXYL MOIETIES.
- 1c4v: SELECTIVE NON ELECTROPHILIC THROMBIN INHIBITORS WITH CYCLOHEXYL MOIETIES.
- 1c4y: SELECTIVE NON-ELECTROPHILIC THROMBIN INHIBITORS
- 1c5l: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR
- 1c5n: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR
- 1c5o: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR
- 1ca8: THROMBIN INHIBITORS WITH RIGID TRIPEPTIDYL ALDEHYDES
- 1d3d: CRYSTAL STRUCTURE OF HUMAN ALPHA THROMBIN IN COMPLEX WITH BENZOTHIOPHENE INHIBITOR 4
- 1d3p: CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN IN COMPLEX WITH BENZO[B]THIOPHENE INHIBITOR 3
- 1d3q: CRYSTAL STRUCTURE OF HUMAN ALPHA THROMBIN IN COMPLEX WITH BENZO[B]THIOPHENE INHIBITOR 2
- 1d3t: CRYSTAL STRUCTURE OF HUMAN ALPHA THROMBIN IN COMPLEX WITH BENZO[B]THIOPHENE INHIBITOR 1
- 1d4p: CRYSTAL STRUCTURE OF HUMAN ALPHA THROMBIN IN COMPLEX WITH 5-AMIDINOINDOLE-4-BENZYLPIPERIDINE INHIBITOR
- 1d6w: STRUCTURE OF THROMBIN COMPLEXED WITH SELECTIVE NON-ELECTROPHILIC INHIBITORS HAVING CYCLOHEXYL MOIETIES AT P1
- 1d9i: STRUCTURE OF THROMBIN COMPLEXED WITH SELECTIVE NON-ELECTOPHILIC INHIBITORS HAVING CYCLOHEXYL MOIETIES AT P1
- 1de7: INTERACTION OF FACTOR XIII ACTIVATION PEPTIDE WITH ALPHA-THROMBIN: CRYSTAL STRUCTURE OF THE ENZYME-SUBSTRATE COMPLEX
- 1dit: COMPLEX OF A DIVALENT INHIBITOR WITH THROMBIN
- 1dm4: SER195ALA MUTANT OF HUMAN THROMBIN COMPLEXED WITH FIBRINOPEPTIDE A (7-16)
- 1doj: Crystal structure of human alpha-thrombin*RWJ-51438 complex at 1.7 A
- 1dwb: CRYSTALLOGRAPHIC ANALYSIS AT 3.0-ANGSTROMS RESOLUTION OF THE BINDING TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS
- 1dwc: CRYSTALLOGRAPHIC ANALYSIS AT 3.0-ANGSTROMS RESOLUTION OF THE BINDING TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS
- 1dwd: CRYSTALLOGRAPHIC ANALYSIS AT 3.0-ANGSTROMS RESOLUTION OF THE BINDING TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS
- 1dwe: CRYSTALLOGRAPHIC ANALYSIS AT 3.0-ANGSTROMS RESOLUTION OF THE BINDING TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS
- 1dx5: CRYSTAL STRUCTURE OF THE THROMBIN-THROMBOMODULIN COMPLEX
- 1e0f: CRYSTAL STRUCTURE OF THE HUMAN ALPHA-THROMBIN-HAEMADIN COMPLEX: AN EXOSITE II-BINDING INHIBITOR
- 1eb1: COMPLEX STRUCTURE OF HUMAN THROMBIN WITH N-METHYL-ARGININE INHIBITOR
- 1eoj: DESIGN OF P1' AND P3' RESIDUES OF TRIVALENT THROMBIN INHIBITORS AND THEIR CRYSTAL STRUCTURES
- 1eol: DESIGN OF P1' AND P3' RESIDUES OF TRIVALENT THROMBIN INHIBITORS AND THEIR CRYSTAL STRUCTURES
- 1fpc: ACTIVE SITE MIMETIC INHIBITION OF THROMBIN
- 1fph: THE INTERACTION OF THROMBIN WITH FIBRINOGEN: A STRUCTURAL BASIS FOR ITS SPECIFICITY
- 1g30: THROMBIN INHIBITOR COMPLEX
- 1g32: THROMBIN INHIBITOR COMPLEX
- 1g37: CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN COMPLEXED WITH BCH-10556 AND EXOSITE-DIRECTED PEPTIDE
- 1ghv: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE
- 1ghw: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE
- 1ghx: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE
- 1ghy: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE
- 1gj4: SELECTIVITY AT S1, H2O DISPLACEMENT, UPA, TPA, SER190/ALA190 PROTEASE, STRUCTURE-BASED DRUG DESIGN
- 1gj5: SELECTIVITY AT S1, H2O DISPLACEMENT, UPA, TPA, SER190/ALA190 PROTEASE, STRUCTURE-BASED DRUG DESIGN
- 1h8d: X-RAY STRUCTURE OF THE HUMAN ALPHA-THROMBIN COMPLEX WITH A TRIPEPTIDE PHOSPHONATE INHIBITOR.
- 1h8i: X-RAY CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN WITH A TRIPEPTIDE PHOSPHONATE INHIBITOR.
- 1hag: THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2, HIRUGEN-AND PPACK-THROMBIN: CHANGES ACCOMPANYING ACTIVATION AND EXOSITE BINDING TO THROMBIN
- 1hah: THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2, HIRUGEN-AND PPACK-THROMBIN: CHANGES ACCOMPANYING ACTIVATION AND EXOSITE BINDING TO THROMBIN
- 1hai: THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2, HIRUGEN-AND PPACK-THROMBIN: CHANGES ACCOMPANYING ACTIVATION AND EXOSITE BINDING TO THROMBIN
- 1hao: COMPLEX OF HUMAN ALPHA-THROMBIN WITH A 15MER OLIGONUCLEOTIDE GGTTGGTGTGGTTGG (BASED ON NMR MODEL OF DNA
- 1hap: COMPLEX OF HUMAN ALPHA-THROMBIN WITH A 15MER OLIGONUCLEOTIDE GGTTGGTGTGGTTGG (BASED ON X-RAY MODEL OF DNA)
- 1hbt: HUMAN ALPHA-THROMBIN COMPLEXED WITH A PEPTIDYL PYRIDINIUM METHYL KETONE CONTAINING BIVALENT INHIBITOR
- 1hdt: STRUCTURE OF A RETRO-BINDING PEPTIDE INHIBITOR COMPLEXED WITH HUMAN ALPHA-THROMBIN
- 1hgt: STRUCTURE OF THE HIRUGEN AND HIRULOG 1 COMPLEXES OF ALPHA-THROMBIN
- 1hlt: THE STRUCTURE OF A NONADECAPEPTIDE OF THE FIFTH EGF DOMAIN OF THROMBOMODULIN COMPLEXED WITH THROMBIN
- 1hut: THE STRUCTURE OF ALPHA-THROMBIN INHIBITED BY A 15-MER SINGLE-STRANDED DNA APTAMER
- 1hxe: SERINE PROTEASE
- 1hxf: HUMAN THROMBIN COMPLEX WITH HIRUDIN VARIANT
- 1ihs: CRYSTAL STRUCTURE OF THE COMPLEX OF HUMAN ALPHA-THROMBIN AND NON-HYDROLYZABLE BIFUNCTIONAL INHIBITORS, HIRUTONIN-2 AND HIRUTONIN-6
- 1iht: CRYSTAL STRUCTURE OF THE COMPLEX OF HUMAN ALPHA-THROMBIN AND NON-HYDROLYZABLE BIFUNCTIONAL INHIBITORS, HIRUTONIN-2 AND HIRUTONIN-6
- 1jmo: Crystal Structure of the Heparin Cofactor II-S195A Thrombin Complex
- 1jou: Crystal Structure of Native S195A Thrombin with an Unoccupied Active Site
- 1jwt: CRYSTAL STRUCTURE OF THROMBIN IN COMPLEX WITH A NOVEL BICYCLIC LACTAM INHIBITOR
- 1k21: HUMAN THROMBIN-INHIBITOR COMPLEX
- 1k22: HUMAN THROMBIN-INHIBITOR COMPLEX
- 1kts: Thrombin Inhibitor Complex
- 1ktt: Thrombin inhibitor complex
- 1lhc: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROARG-OH
- 1lhd: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROLYS-OH
- 1lhe: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BORO-N-BUTYL-AMIDINO-GLYCINE-OH
- 1lhf: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BORO-HOMOLYS-OH
- 1lhg: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROORNITHINE-OH
- 1mh0: Crystal structure of the anticoagulant slow form of thrombin
- 1mu6: Crystal Structure of Thrombin in Complex with L-378,622
- 1mu8: thrombin-hirugen_l-378,650
- 1mue: Thrombin-Hirugen-L405,426
- 1nm6: thrombin in complex with selective macrocyclic inhibitor at 1.8A
- 1no9: Design of weakly basic thrombin inhibitors incorporating novel P1 binding functions: molecular and X-ray crystallographic studies.
- 1nrn: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES
- 1nro: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES
- 1nrp: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES
- 1nrq: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES
- 1nrr: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES
- 1nrs: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES
- 1nt1: thrombin in complex with selective macrocyclic inhibitor
- 1nu7: Staphylocoagulase-Thrombin Complex
- 1nu9: Staphylocoagulase-Prethrombin-2 complex
- 1ny2: Human alpha thrombin inhibited by RPPGF and hirugen
- 1nzq: D-Phe-Pro-Arg-Type Thrombin Inhibitor
- 1o0d: Human Thrombin complexed with a d-Phe-Pro-Arg-type Inhibitor and a C-terminal Hirudin derived exo-site inhibitor
- 1o2g: Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors
- 1o5g: Dissecting and Designing Inhibitor Selectivity Determinants at the S1 site Using an Artificial Ala190 Protease (Ala190 uPA)
- 1ook: Crystal Structure of the Complex of Platelet Receptor GPIb-alpha and Human alpha-Thrombin
- 1oyt: COMPLEX OF RECOMBINANT HUMAN THROMBIN WITH A DESIGNED FLUORINATED INHIBITOR
- 1p8v: CRYSTAL STRUCTURE OF THE COMPLEX OF PLATELET RECEPTOR GPIB-ALPHA AND ALPHA-THROMBIN AT 2.6A
- 1ppb: THE REFINED 1.9 ANGSTROMS CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN: INTERACTION WITH D-PHE-PRO-ARG CHLOROMETHYLKETONE AND SIGNIFICANCE OF THE TYR-PRO-PRO-TRP INSERTION SEGMENT
- 1qbv: CRYSTAL STRUCTURE OF THROMBIN COMPLEXED WITH AN GUANIDINE-MIMETIC INHIBITOR
- 1qhr: NOVEL COVALENT ACTIVE SITE THROMBIN INHIBITORS
- 1qj1: NOVEL COVALENT ACTIVE SITE THROMBIN INHIBITORS
- 1qj6: NOVEL COVALENT ACTIVE SITE THROMBIN INHIBITORS
- 1qj7: NOVEL COVALENT ACTIVE SITE THROMBIN INHIBITORS
- 1qur: HUMAN ALPHA-THROMBIN IN COMPLEX WITH BIVALENT, BENZAMIDINE-BASED SYNTHETIC INHIBITOR
- 1rd3: 2.5A Structure of Anticoagulant Thrombin Variant E217K
- 1riw: Thrombin in complex with natural product inhibitor Oscillarin
- 1sb1: Novel Non-Covalent Thrombin Inhibitors Incorporating P1 4,5,6,7-Tetrahydrobenzothiazole Arginine Side Chain Mimetics
- 1sfq: Fast form of thrombin mutant R(77a)A bound to PPACK
- 1sgi: Crystal structure of the anticoagulant slow form of thrombin
- 1shh: Slow form of Thrombin Bound with PPACK
- 1sl3: crystal structure of Thrombin in complex with a potent P1 heterocycle-Aryl based inhibitor
- 1sr5: ANTITHROMBIN-ANHYDROTHROMBIN-HEPARIN TERNARY COMPLEX STRUCTURE
- 1t4u: Crystal Structure Analysis of a novel Oxyguanidine bound to Thrombin
- 1t4v: Crystal Structure Analysis of a novel Oxyguanidine bound to Thrombin
- 1ta2: Crystal structure of thrombin in complex with compound 1
- 1ta6: Crystal structure of thrombin in complex with compound 14b
- 1tb6: 2.5A Crystal Structure of the Antithrombin-Thrombin-Heparin Ternary Complex
- 1tbz: HUMAN THROMBIN WITH ACTIVE SITE N-METHYL-D PHENYLALANYL-N-[5-(AMINOIMINOMETHYL)AMINO]-1-[(BENZOTHIAZOLYL)CARBONYL] BUTYL]-L-PROLINAMIDE TRIFLUROACETATE AND EXOSITE-HIRUGEN
- 1thp: STRUCTURE OF HUMAN ALPHA-THROMBIN Y225P MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE
- 1thr: STRUCTURES OF THROMBIN COMPLEXES WITH A DESIGNED AND A NATURAL EXOSITE INHIBITOR
- 1ths: STRUCTURES OF THROMBIN COMPLEXES WITH A DESIGNED AND A NATURAL EXOSITE INHIBITOR
- 1tmb: MOLECULAR BASIS FOR THE INHIBITION OF HUMAN ALPHA-THROMBIN BY THE MACROCYCLIC PEPTIDE CYCLOTHEONAMIDE A
- 1tmt: CHANGES IN INTERACTIONS IN COMPLEXES OF HIRUDIN DERIVATIVES AND HUMAN ALPHA-THROMBIN DUE TO DIFFERENT CRYSTAL FORMS
- 1tmu: CHANGES IN INTERACTIONS IN COMPLEXES OF HIRUDIN DERIVATIVES AND HUMAN ALPHA-THROMBIN DUE TO DIFFERENT CRYSTAL FORMS
- 1tom: ALPHA-THROMBIN COMPLEXED WITH HIRUGEN
- 1tq0: Crystal structure of the potent anticoagulant thrombin mutant W215A/E217A in free form
- 1tq7: Crystal structure of the anticoagulant thrombin mutant W215A/E217A bound to PPACK
- 1twx: Crystal structure of the thrombin mutant D221A/D222K
- 1ucy: THROMBIN COMPLEXED WITH FIBRINOPEPTIDE A ALPHA (RESIDUES 7-19). THREE COMPLEXES, ONE WITH EPSILON-THROMBIN AND TWO WITH ALPHA-THROMBIN
- 1uma: ALPHA-THROMBIN (HIRUGEN) COMPLEXED WITH NA-(N,N-DIMETHYLCARBAMOYL)-ALPHA-AZALYSINE
- 1uvs: BOVINE THROMBIN--BM51.1011 COMPLEX
- 1vit: THROMBIN:HIRUDIN 51-65 COMPLEX
- 1vr1: Specificity for Plasminogen Activator Inhibitor-1
- 1vzq: COMPLEX OF THROMBIN WITH DESIGNED INHIBITOR 7165
- 1w7g: ALPHA-THROMBIN COMPLEX WITH SULFATED HIRUDIN (RESIDUES 54-65) AND L-ARGININE TEMPLATE INHIBITOR CS107
- 1way: ACTIVE SITE THROMBIN INHIBITORS
- 1wbg: ACTIVE SITE THROMBIN INHIBITORS
- 1xm1: Nonbasic Thrombin Inhibitor Complex
- 1xmn: Crystal structure of thrombin bound to heparin
- 1ycp: THE CRYSTAL STRUCTURE OF FIBRINOGEN-AA PEPTIDE 1-23 (F8Y) BOUND TO BOVINE THROMBIN EXPLAINS WHY THE MUTATION OF PHE-8 TO TYROSINE STRONGLY INHIBITS NORMAL CLEAVAGE AT ARGININE-16
- 1ype: Thrombin Inhibitor Complex
- 1ypg: Thrombin Inhibitor Complex
- 1ypj: Thrombin Inhibitor Complex
- 1ypk: Thrombin Inhibitor Complex
- 1ypl: X-ray crystal structure of thrombin inhibited by synthetic cyanopeptide analogue RA-1008
- 1ypm: X-ray crystal structure of thrombin inhibited by synthetic cyanopeptide analogue RA-1014
- 1z71: thrombin and P2 pyridine N-oxide inhibitor complex structure
- 1z8i: Crystal structure of the thrombin mutant G193A bound to PPACK
- 1z8j: Crystal structure of the thrombin mutant G193P bound to PPACK
- 1zgi: thrombin in complex with an oxazolopyridine inhibitor 21
- 1zgv: Thrombin in complex with an oxazolopyridine inhibitor 2
- 1zrb: Thrombin in complex with an azafluorenyl inhibitor 23b
- 2a0q: Structure of thrombin in 400 mM potassium chloride
- 2a2x: Orally Active Thrombin Inhibitors in Complex with Thrombin Inh12
- 2a45: Crystal structure of the complex between thrombin and the central ""E"" region of fibrin
- 2afq: 1.9 angstrom crytal structure of wild-type human thrombin in the sodium free state
- 2ank: orally active thrombin inhibitors in complex with thrombin and an exosite decapeptide
- 2anm: Ternary complex of an orally active thrombin inhibitor with human thrombin and a c-terminal hirudin derived exo-sit inhibitor
- 2b5t: 2.1 Angstrom structure of a nonproductive complex between antithrombin, synthetic heparin mimetic SR123781 and two S195A thrombin molecules
- 2bdy: thrombin in complex with inhibitor
- 2bvr: HUMAN THROMBIN COMPLEXED WITH FRAGMENT-BASED SMALL MOLECULES OCCUPYING THE S1 POCKET
- 2bvs: HUMAN THROMBIN COMPLEXED WITH FRAGMENT-BASED SMALL MOLECULES OCCUPYING THE S1 POCKET
- 2bvx: DESIGN AND DISCOVERY OF NOVEL, POTENT THROMBIN INHIBITORS WITH A SOLUBILIZING CATIONIC P1-P2-LINKER
- 2bxt: DESIGN AND DISCOVERY OF NOVEL, POTENT THROMBIN INHIBITORS WITH A SOLUBILIZING CATIONIC P1-P2-LINKER
- 2bxu: DESIGN AND DISCOVERY OF NOVEL, POTENT THROMBIN INHIBITORS WITH A SOLUBILIZING CATIONIC P1-P2-LINKER
- 2c8w: THROMBIN INHIBITORS
- 2c8x: THROMBIN INHIBITORS
- 2c8y: THROMBIN INHIBITORS
- 2c8z: THROMBIN INHIBITORS
- 2c90: THROMBIN INHIBITORS
- 2c93: THROMBIN INHIBITORS
- 2cf8: COMPLEX OF RECOMBINANT HUMAN THROMBIN WITH A INHIBITOR
- 2cf9: COMPLEX OF RECOMBINANT HUMAN THROMBIN WITH A INHIBITOR
- 2cn0: COMPLEX OF RECOMBINANT HUMAN THROMBIN WITH A DESIGNED INHIBITOR
- 2feq: orally active thrombin inhibitors
- 2fes: Orally active thrombin inhibitors
- 2gde: Thrombin in complex with inhibitor
- 2gp9: Crystal structure of the slow form of thrombin in a self-inhibited conformation
- 2h9t: Crystal structure of human alpha-thrombin in complex with suramin
- 2hgt: STRUCTURE OF THE HIRUGEN AND HIRULOG 1 COMPLEXES OF ALPHA-THROMBIN
- 2hnt: CRYSTALLOGRAPHIC STRUCTURE OF HUMAN GAMMA-THROMBIN
- 2hpp: STRUCTURES OF THE NONCOVALENT COMPLEXES OF HUMAN AND BOVINE PROTHROMBIN FRAGMENT 2 WITH HUMAN PPACK-THROMBIN
- 2hpq: STRUCTURES OF THE NONCOVALENT COMPLEXES OF HUMAN AND BOVINE PROTHROMBIN FRAGMENT 2 WITH HUMAN PPACK-THROMBIN
- 2hwl: Crystal structure of thrombin in complex with fibrinogen gamma' peptide
- 2jh0: HUMAN THROMBIN HIRUGEN INHIBITOR COMPLEX.
- 2jh5: HUMAN THROMBIN HIRUGEN INHIBITOR COMPLEX.
- 2jh6: HUMAN THROMBIN HIRUGEN INHIBITOR COMPLEX.
- 2od3: Human thrombin chimera with human residues 184a, 186, 186a, 186b, 186c and 222 replaced by murine thrombin equivalents.
- 2thf: STRUCTURE OF HUMAN ALPHA-THROMBIN Y225F MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE
- 3hat: ACTIVE SITE MIMETIC INHIBITION OF THROMBIN
- 4htc: THE REFINED STRUCTURE OF THE HIRUDIN-THROMBIN COMPLEX
- 4thn: THE CRYSTAL STRUCTURE OF ALPHA-THROMBIN-HIRUNORM IV COMPLEX REVEALS A NOVEL SPECIFICITY SITE RECOGNITION MODE.
- 5gds: HIRUNORMS ARE TRUE HIRUDIN MIMETICS. THE CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN:HIRUNORM V COMPLEX
- 7kme: CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN INHIBITED WITH SEL2711.
- 8kme: CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN INHIBITED WITH SEL2770.