Extended and bent conformations of the mannose receptor family |
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Authors: | O Llorca |
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Institution: | (1) Centro de Investigaciones Biológicas, Spanish National Research Council (CSIC), Ramiro de Maeztu 9, Campus Universidad Complutense, Madrid, 28040, Spain |
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Abstract: | In mammals, the mannose receptor family consists of four members, Endo180, DEC-205, phospholipase A2 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 threedimensional 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.
Received 25 October 2007; received after revision 23 November 2007; accepted 7 December 2007 |
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Keywords: | Mannose receptor Endo180 DEC-205 phospholipase A2 receptor conformation electron microscopy |
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