Determinants of laminin polymerization revealed by the structure of the α5 chain amino-terminal region

被引：56

作者：

Hussain, Sadaf-Ahmahni ^{[1
]}

Carafoli, Federico ^{[1
]}

Hohenester, Erhard ^{[1
]}

机构：

[1] Univ London Imperial Coll Sci Technol & Med, Blackett Lab, Dept Life Sci, London SW7 2AZ, England

来源：

EMBO REPORTS | 2011年 / 12卷 / 03期

基金：

英国惠康基金; 英国生物技术与生命科学研究理事会;

关键词：

basement membrane; LN domain; netrin; X-ray crystallography; MUSCULAR-DYSTROPHY; CRYSTAL-STRUCTURE; BINDING SITES; DOMAINS; MUTATION; MODULES;

D O I：

10.1038/embor.2011.3

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：

The polymerization of laminin into a cell-associated network-a key step in basement membrane assembly-is mediated by the laminin amino-terminal (LN) domains at the tips of the three short arms of the laminin alpha beta gamma-heterotrimer. The crystal structure of a laminin alpha 5LN-LE1-2 fragment shows that the LN domain is a beta-jelly roll with several elaborate insertions that is attached like a flower head to the stalk-like laminin-type epidermal growth factor-like tandem. A surface loop that is strictly conserved in the LN domains of all alpha-short arms is required for stable ternary association with the beta- and gamma-short arms in the laminin network.

引用

页码：276 / 282

页数：7

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