凝血因子VIIa与可溶性组织因子复合物的晶体结构

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

作者信息

Banner D W, D'Arcy A, Chène C, Winkler F K, Guha A, Konigsberg W H, Nemerson Y, Kirchhofer D

机构信息

Pharma Division, F. Hoffmann-La Roche, Basle, Switzerland.

出版信息

Nature. 1996 Mar 7;380(6569):41-6. doi: 10.1038/380041a0.

DOI:10.1038/380041a0

PMID:8598903

Abstract

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.

摘要

当组织因子与凝血因子VIIa结合形成一种具有酶活性的复合物时，血液凝固过程启动，该复合物随后激活因子IX和X，导致凝血酶生成和血栓形成。我们已经确定了活性位点被抑制的因子VIIa与组织因子裂解的细胞外结构域形成的复合物在2.0埃分辨率下的晶体结构。在该复合物中，因子VIIa呈现出伸展构象。这一结构为理解凝血起始的许多分子层面提供了基础。