Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X

被引：119

作者：

Mizuno, H ^{[1
]}

Fujimoto, Z

Atoda, H

Morita, T

机构：

[1] Natl Inst Agrobiol Resources, Dept Biotechnol, Tsukuba, Ibaraki 3058602, Japan

[2] Meiji Pharmaceut Univ, Dept Biochem, Tokyo 2048588, Japan

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2001年 / 98卷 / 13期

关键词：

D O I：

10.1073/pnas.131179698

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：

The gamma -carboxyglutamic acid (Gla) domain of blood coagulation factors is responsible for Ca2+-dependent phospholipid membrane binding. Factor X-binding protein (X-bp), an anticoagulant protein from snake venom, specifically binds to the cia domain of factor X. The crystal structure of X-bp in complex with the Gla domain peptide of factor X at 2.3-Angstrom resolution showed that the anticoagulation is based on the fact that two patches of the cia domain essential for membrane binding are buried in the complex formation. The Gla domain thus is expected to be a new target of anticoagulant drugs, and X-bp provides a basis for designing them. This structure also provides a membrane-bound model of factor X.

引用

页码：7230 / 7234

页数：5

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