1dan: Difference between revisions
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==Overview== | ==Overview== | ||
Blood coagulation is initiated when tissue factor binds to coagulation, factor VIIa to give an enzymatically active complex which then activates, factors IX and X, leading to thrombin generation and clot formation. We, have determined the crystal structure at 2.0-A degrees resolution of, active-site-inhibited factor VIIa complexed with the cleaved extracellular, domain of tissue factor. In the complex, factor VIIa adopts an extended, conformation. This structure provides a basis for understanding many, molecular aspects of the initiation of coagulation. | Blood coagulation is initiated when tissue factor binds to coagulation, factor VIIa to give an enzymatically active complex which then activates, factors IX and X, leading to thrombin generation and clot formation. We, have determined the crystal structure at 2.0-A degrees resolution of, active-site-inhibited factor VIIa complexed with the cleaved extracellular, domain of tissue factor. In the complex, factor VIIa adopts an extended, conformation. This structure provides a basis for understanding many, molecular aspects of the initiation of coagulation. | ||
''Page seeded by [http://bip.weizmann.ac.il/oca OCA ] on Thu Oct 25 | ==Reference== | ||
The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor., Banner DW, D'Arcy A, Chene C, Winkler FK, Guha A, Konigsberg WH, Nemerson Y, Kirchhofer D, Nature. 1996 Mar 7;380(6569):41-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8598903 8598903] | |||
[[Category: Banner, D.W.]] | |||
''Page seeded by [http://bip.weizmann.ac.il/oca OCA ] on Thu Oct 25 14:20:59 2007'' | |||
