Crystal structure of the factor XI zymogen reveals a pathway for transactivation

被引：96

作者：

Papagrigoriou, Evangelos

McEwan, Paul A.

Walsh, Peter N.

Emsley, Jonas ^{[1
]}

机构：

[1] Univ Nottingham, Sch Pharm, Ctr Biomol Sci, Nottingham NG7 2RD, England

[2] Temple Univ, Sch Med, Fels Inst Canc Res, Dept Med,Dept Biochem,Sol Sherry Thrombosis Res C, Philadelphia, PA 19140 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2006年 / 13卷 / 06期

基金：

英国惠康基金;

关键词：

D O I：

10.1038/nsmb1095

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：

Factor XI (FXI), a coagulation protein essential to normal hemostasis, circulates as a disulfide-linked dimer. Here we report the full-length FXI zymogen crystal structure, revealing that the protease and four apple domains assemble into a unique 'cup and saucer' architecture. The structure shows that the thrombin and platelet glycoprotein Ib binding sites are remote within the monomer but lie in close proximity across the dimer, suggesting a transactivation mechanism.

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页码：557 / 558

页数：2

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