Structure-function studies on β2-glycoprotein I

被引：14

作者：

de Groot, PG ^{[1
]}

Bouma, B

Lutters, BCH

Simmelink, MJA

Derksen, RHWM

Gros, P

机构：

[1] Univ Utrecht, Ctr Med, Haemostasis & Thrombosis Lab, Utrecht, Netherlands

[2] Univ Utrecht, Dept Crystal & Struct Chem, Utrecht, Netherlands

来源：

JOURNAL OF AUTOIMMUNITY | 2000年 / 15卷 / 02期

关键词：

beta(2)-glycoprotein I; antiphospholipid antibodies; phospholipids; lupus anticoagulants; crystal structure;

D O I：

10.1006/jaut.2000.0394

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Human beta 2-glycoprotein I is a heavily glycosylated plasma protein which has been implicated in the binding of antiphospholipid antibodies to negatively charged phospholipids; a process considered as an important risk factor fur the development of thrombosis. We have solved the crystal structure of beta 2-glycoprotein I. In this review we will discuss what the three-dimensional structure teaches us about the role of beta 2-glycoprotein I in the pathogenesis of the antiphospholipid syndrome. (C) 2000 Academic Press.

引用

页码：87 / 89

页数：3

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