Structural basis of collagen recognition by integrin α2β1

被引：919

作者：

Emsley, J

Knight, CG

Farndale, RW

Barnes, MJ

Liddington, RC ^{[1
]}

机构：

[1] Univ Leicester, Dept Biochem, Leicester LE1 7RH, Leics, England

[2] Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England

[3] Burnham Inst, La Jolla, CA 92037 USA

来源：

CELL | 2000年 / 101卷 / 01期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/S0092-8674(00)80622-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

We have determined the crystal structure of a complex between the I domain of integrin alpha 2 beta 1 and a triple helical collagen peptide containing a critical GFOGER motif. Three loops on the upper surface of the I domain that coordinate a metal ion also engage the collagen, with a collagen glutamate completing the coordination sphere of the metal. Comparison with the unliganded I domain reveals a change in metal coordination linked to a reorganization of the upper surface that together create a complementary surface for binding collagen. Conformational changes propagate from the upper surface to the opposite pole of the domain, suggesting both a basis for affinity regulation and a pathway for signal transduction. The structural features observed here may represent a general mechanism for integrin-ligand recognition.

引用

收藏

页码：47 / 56

页数：10

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