The interaction of activated factor VII with tissue factor: insight into the mechanism of cofactor-mediated activation of activated factor VII

被引：0

作者：

Ruf, W

机构：

[1] Scripps Res Inst, Dept Immunol, La Jolla, CA 92037 USA

[2] Scripps Res Inst, Dept Vasc Biol, La Jolla, CA 92037 USA

来源：

BLOOD COAGULATION & FIBRINOLYSIS | 1998年 / 9卷

关键词：

tissue factor; factor VIIa; TF-FVIIa complex formation; serine protease allosteric activation; extended substrate recognition;

D O I：

暂无

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

The structure solution of the complex of tissue factor (TF) and activated factor VII (FVIIa) and extensive mutagenesis analysis of the FVIIa protease domain have recently provided a detailed, novel insight into the function of the extrinsic activation complex. This overview relates the functional data to the known molecular interactions defined by crystallography arriving at a hypothesis of how FVIIa is 'switched on' through specific contacts with TF. Combining these findings with the results of mutational analysis of TF, a picture emerges whereby multiple domains of both cofactor and enzyme provide contacts for the assembly of macromolecular substrate. Blood Coag Fibrinol 9 (suppl 1):S73-S78 (C) 1998 Lippincott-Raven Publishers

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页码：S73 / S78

页数：6

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