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Título

Extended and bent conformations of the mannose receptor family

Autor Llorca, Óscar
Palabras clave Mannose receptor
Endo180
DEC-205
Phospholipase A2 receptor
Conformation
Electron microscopy
Fecha de publicación 12-ene-2008
EditorBirkhäuser Verlag
Springer
Citación Cellular and Molecular Life Sciences 65(9): 1302-1310 (2008)
ResumenIn 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.
Descripción 9 pages, 4 figures.-- PMID: 18193159 [PubMed].-- Printed version published May 2008.
Versión del editorhttp://dx.doi.org/10.1007/s00018-007-7497-9
URI http://hdl.handle.net/10261/9573
DOI10.1007/s00018-007-7497-9
ISSN1420-682X (Print)
1420-9071 (Online)
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