2gfe
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2gfe.gif|left|200px]] | [[Image:2gfe.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2gfe", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2gfe| PDB=2gfe | SCENE= }} | |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''Crystal structure of the GluR2 A476E S673D Ligand Binding Core Mutant at 1.54 Angstroms Resolution''' | '''Crystal structure of the GluR2 A476E S673D Ligand Binding Core Mutant at 1.54 Angstroms Resolution''' | ||
| Line 26: | Line 23: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Mayer, M L.]] | [[Category: Mayer, M L.]] | ||
| - | [[Category: | + | [[Category: Membrane protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:02:48 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:02, 4 May 2008
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. 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 Page seeded by OCA on Sun May 4 05:02:48 2008
