Sandbox Reserved 348
| This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada. |
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| 1ppb, resolution 1.92Å (default scene) | |||||||||||||
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| Ligands: | 0G6 | ||||||||||||
| Activity: | Thrombin, with EC number 3.4.21.5 | ||||||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||

Thrombin is a trypsin-like serine protease which is best known for its role in blood clotting. In humans, the F2 gene codes for prothrombin, which is also known as Coagulation Factor II.[1][2] Clevage of prothrombin to form activated α-thrombin is a key step in the final common pathway of blood clotting, because thrombin activates fibrin, which creates cross-linked fibrin clots.[3]
Structure
Thrombin is comprised of two chains, often referred to as the short chain and the long chain. There is one active site, which in the case of 1ppb is occupied with D-Phe-Pro-Arg chloromethylketone.[4] Additionally, there are three structural disulfide bonds.
3D Structures
α-Thrombin
Prothrombin
See Also
External Resources
- Thrombin at Wikipedia
- Serine protease at Wikipedia
- Fibrin Glue at Wikipedia
- Coagulation (blood clotting) at Wikipedia
- Hemophilia at Wikipedia
References
- ↑ Royle NJ, Irwin DM, Koschinsky ML, MacGillivray RT, Hamerton JL. Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively. Somat Cell Mol Genet. 1987 May;13(3):285-92. PMID:3474786
- ↑ Degen SJ, Davie EW. Nucleotide sequence of the gene for human prothrombin. Biochemistry. 1987 Sep 22;26(19):6165-77. PMID:2825773
- ↑ Di Cera E. Thrombin interactions. Chest. 2003 Sep;124(3 Suppl):11S-7S. PMID:12970119
- ↑ Bode W, Mayr I, Baumann U, Huber R, Stone SR, Hofsteenge J. The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J. 1989 Nov;8(11):3467-75. PMID:2583108
