Three-dimensional interplay among the ligand-binding domains of the urokinase-plasminogen-activator-receptor-associated protein, Endo180

被引:20
作者
Rivera-Calzada, A
Robertson, D
MacFadyen, JR
Boskovic, J
Isacke, CM
Llorca, O
机构
[1] CSIC, Ctr Invest Biol, Madrid 28040, Spain
[2] Inst Canc Res, Chester Beatty Labs, Breakthrough Toby Robins Breast Canc Res Ctr, London SW3 6JB, England
关键词
D O I
10.1038/sj.embor.embor898
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
Endo180, also known as the urokinase plasminogen activator receptor (uPAR)-associated protein ( uPARAP), is one of the four members of the mannose receptor family, and is implicated in extracellular-matrix remodelling through its interactions with collagens, sugars and uPAR. The extracellular portion of Endo180 contains an amino-terminal cysteine-rich domain, a single fibronectin type II domain and eight C-type lectin-like domains. We have purified a soluble version of Endo180 and analysed it by single-particle electron microscopy to obtain a three-dimensional structure of the N-terminal part of the protein at a resolution of 17 Angstrom and reveal, for the first time, the interactions between non-adjacent domains in the mannose receptor family. We show that for Endo180, the cysteine-rich domain contacts the second C-type lectin-like domain, thus providing structural insight into how modulation of its several ligand interactions may regulate Endo180 receptor function.
引用
收藏
页码:807 / 812
页数:6
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