The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor

被引：676

作者：

Banner, DW

DArcy, A

Chene, C

Winkler, FK

Guha, A

Konigsberg, WH

Nemerson, Y

Kirchhofer, D

机构：

[1] CUNY MT SINAI SCH MED, DEPT MED, NEW YORK, NY 10029 USA

[2] CUNY MT SINAI SCH MED, DEPT BIOCHEM, NEW YORK, NY 10029 USA

[3] YALE UNIV, DEPT MOLEC BIOPHYS & BIOCHEM, NEW HAVEN, CT 06510 USA

来源：

NATURE | 1996年 / 380卷 / 6569期

关键词：

D O I：

10.1038/380041a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 too thrombin generation and clot formation. We have determined the crystal structure at 2.0-Angstrom 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.

引用

页码：41 / 46

页数：6

共 51 条

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