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

Abstract:

: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 A 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.

journal_name

EMBO Rep

journal_title

EMBO reports

authors

Rivera-Calzada A,Robertson D,MacFadyen JR,Boskovic J,Isacke CM,Llorca O

doi

10.1038/sj.embor.embor898

keywords:

subject

Has Abstract

pub_date

2003-08-01 00:00:00

pages

807-12

issue

8

eissn

1469-221X

issn

1469-3178

pii

embor898

journal_volume

4

pub_type

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