2gfe
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(New page: 200px<br /><applet load="2gfe" size="350" color="white" frame="true" align="right" spinBox="true" caption="2gfe, resolution 1.54Å" /> '''Crystal structure of...)
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Revision as of 17:58, 29 January 2008
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Crystal structure of the GluR2 A476E S673D Ligand Binding Core Mutant at 1.54 Angstroms Resolution
Overview
Ionotropic glutamate receptors perform diverse functions in the nervous, system. As a result, multiple receptor subtypes have evolved with, different kinetics, ion permeability, expression patterns, and regulation, by second messengers. Kainate receptors show slower recovery from, desensitization and have different affinities for agonists than AMPA, receptors. Based on analysis of ligand binding domain crystal structures, we identified interdomain interactions in the agonist-bound state that are, conserved in kainate receptors and absent in AMPA receptors. Mutations in, GluR6 designed to disrupt these contacts reduced agonist apparent, affinity, speeded up receptor deactivation and increased the rate of, recovery from desensitization. Conversely, introduction of mutations in, GluR2 that enabled additional interdomain interactions in the, agonist-bound state increased agonist apparent affinity 15-fold, and, slowed both deactivation and recovery from desensitization. We conclude, that interdomain interactions have evolved as a distinct mechanism that, contributes to the unique kinetic properties of AMPA and kainate, receptors.
About this Structure
2GFE is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Full crystallographic information is available from OCA.
Reference
Interdomain interactions in AMPA and kainate receptors regulate affinity for glutamate., Weston MC, Gertler C, Mayer ML, Rosenmund C, J Neurosci. 2006 Jul 19;26(29):7650-8. PMID:16855092
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