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
引用
收藏
页码：S73 / S78
页数：6
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