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Sandbox Reserved 348
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Thrombin is comprised of two chains, often referred to as the <scene name='Sandbox_Reserved_348/Small_subunit/2'>short chain</scene> and the <scene name='Sandbox_Reserved_348/Large_subunit/2'>long chain</scene>. There is one <scene name='Sandbox_Reserved_348/Ligand/2'>active site</scene>, which in the case of [[1ppb]] is occupied with D-Phe-Pro-Arg chloromethylketone.<ref name="The refined 1.9A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.">PMID:2583108</ref> Additionally, there are three structural disulfide bonds. | Thrombin is comprised of two chains, often referred to as the <scene name='Sandbox_Reserved_348/Small_subunit/2'>short chain</scene> and the <scene name='Sandbox_Reserved_348/Large_subunit/2'>long chain</scene>. There is one <scene name='Sandbox_Reserved_348/Ligand/2'>active site</scene>, which in the case of [[1ppb]] is occupied with D-Phe-Pro-Arg chloromethylketone.<ref name="The refined 1.9A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.">PMID:2583108</ref> Additionally, there are three structural disulfide bonds. | ||
| - | ==3D Structures | + | ==3D Structures== |
| + | ===α-Thrombin=== | ||
*[[1ppb]] | *[[1ppb]] | ||
*[[1uma]] | *[[1uma]] | ||
*[[1de7]] | *[[1de7]] | ||
| - | == | + | ===Prothrombin=== |
*[[2afq]] | *[[2afq]] | ||
Revision as of 05:00, 27 March 2011
| 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. |
To get started:
More help: Help:Editing |
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| 1ppb, resolution 1.92Å () | |||||||||
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| 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]
Contents |
Structure
Thrombin is comprised of two chains, often referred to as the and the . There is one , 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

