2gfe

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{{STRUCTURE_2gfe| PDB=2gfe | SCENE= }}
{{STRUCTURE_2gfe| PDB=2gfe | SCENE= }}
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'''Crystal structure of the GluR2 A476E S673D Ligand Binding Core Mutant at 1.54 Angstroms Resolution'''
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===Crystal structure of the GluR2 A476E S673D Ligand Binding Core Mutant at 1.54 Angstroms Resolution===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16855092 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16855092}}
==About this Structure==
==About this Structure==
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[[Category: Mayer, M L.]]
[[Category: Mayer, M L.]]
[[Category: Membrane protein]]
[[Category: Membrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:02:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:13:38 2008''

Revision as of 03:13, 29 July 2008

Image:2gfe.png

Template:STRUCTURE 2gfe

Crystal structure of the GluR2 A476E S673D Ligand Binding Core Mutant at 1.54 Angstroms Resolution

Template:ABSTRACT PUBMED 16855092

About this Structure

2GFE is a Single protein structure of sequence from Rattus norvegicus. 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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