Structure-function relationships of C-type lectin-related proteins

被引：23
|
作者：
Morita, Takashi [1 ]
机构：
[1] Meiji Pharmaceut Univ, Dept Biochem, Tokyo 2048588, Japan
来源：
PATHOPHYSIOLOGY OF HAEMOSTASIS AND THROMBOSIS | 2005年 / 34卷 / 4-5期
关键词：
C-type lectin-like protein; three-dimensional domain swapping; blood coagulation factor IX/ factor X-binding protein (IX/X-bp); EMS-16; collagen receptor antagonist;
D O I：
10.1159/000092415
中图分类号：
R5 [内科学];
学科分类号：
1002 ; 100201 ;
摘要：
The structural and functional studies of the first identified C-type lectin-like protein (CLP), blood coagulation factor (X/factor X-binding protein (IX/X-bp), have been instrumental in defining how new functionally heterodimeric CLPs are generated from monomeric carbohydrate recognition domain in C-type lectins by three-dimensional domain swapping. The crystal structures of gamma-carboxyglutamic acid domains of coagulation factors X and IX have recently been clarified in structural studies of complexes between the gamma-carboxyglutamic acid domain of factors X and X-bp (a venom CLP) and between the gamma-carboxyglutamic acid domain of factors IX and IX-bp (a venom CLP). Copyright (c) 2005 S. Karger AG, Basel
引用
收藏
页码：156 / 159
页数：4
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