English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/9573
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


Extended and bent conformations of the mannose receptor family

AuthorsLlorca, Óscar
KeywordsMannose receptor
Phospholipase A2 receptor
Electron microscopy
Issue Date12-Jan-2008
PublisherBirkhäuser Verlag
CitationCellular and Molecular Life Sciences 65(9): 1302-1310 (2008)
AbstractIn mammals, the mannose receptor family consists of four members, Endo180, DEC-205, phospholipase A(2) receptor and the mannose receptor. The extracellular domains of all these receptors contain a similar arrangement of domains in which an Nterminal cysteine-rich domain is followed by a single fibronectin type II domain and eight or ten C-type lectin-like domains. This review focuses on the three-dimensional structure of the receptors in the mannose receptor family and its functional implication. Recent research has revealed that several members of this family can exist in at least two configurations: an extended conformation with the N-terminal cysteinerich domain pointing outwards from the cell membrane and a bent conformation where the N-terminal domains fold back to interact with C-type lectin-like domains at the middle of the structure. Conformational transitions between these two states seem to regulate the interaction of these receptors with ligands and their oligomerization.
Description9 pages, 4 figures.-- PMID: 18193159 [PubMed].-- Printed version published May 2008.
Publisher version (URL)http://dx.doi.org/10.1007/s00018-007-7497-9
Appears in Collections:(CIB) Artículos
Files in This Item:
There are no files associated with this item.
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.