ANTITHROMBIN-III - STRUCTURAL AND FUNCTIONAL-ASPECTS

被引：61
|
作者：
MOUREY, L
SAMAMA, JP
DELARUE, M
CHOAY, J
LORMEAU, JC
PETITOU, M
MORAS, D
机构：
[1] INST BIOL MOLEC & CELLULAIRE, CRISTALLOG BIOL LAB, CNRS, 15 RUE RENE DESCARTES, F-67084 STRASBOURG, FRANCE
[2] SANOFI RECH, F-94256 GENTILLY, FRANCE
来源：
BIOCHIMIE | 1990年 / 72卷 / 08期
关键词：
antithrombin III; heparin; serpin superfamily; X-ray structure;
D O I：
10.1016/0300-9084(90)90123-X
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Antithrombin III is a plasma gylcoprotein responsible for thrombin inhibition in the blood coagulation cascade. The X-ray structure of its cleaved form has been determined and refined to 3.2 Å resolution. The overall topology is similar to that of ω1-antitrypsin, another member of the serpin (serine protease inhibitor) superfamily. The biological activity of antithrombin III is mediated by a polysaccharide, heparin. The binding site of this effector is described. A possible structural transition from the native to the cleaved structure is discussed. © 1990.
引用
收藏
页码：599 / 608
页数：10
相关论文
共 50 条
12345