1lb8: Difference between revisions

Revision as of 12:12, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1lb8.png

Template:STRUCTURE 1lb8

Crystal structure of the Non-desensitizing GluR2 ligand binding core mutant (S1S2J-L483Y) in complex with AMPA at 2.3 resolutionCrystal structure of the Non-desensitizing GluR2 ligand binding core mutant (S1S2J-L483Y) in complex with AMPA at 2.3 resolution

Template:ABSTRACT PUBMED 12015593

About this StructureAbout this Structure

1LB8 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Mechanism of glutamate receptor desensitization., Sun Y, Olson R, Horning M, Armstrong N, Mayer M, Gouaux E, Nature. 2002 May 16;417(6886):245-53. PMID:12015593

Page seeded by OCA on Wed Jul 2 12:12:35 2008

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-[[Image:1lb8.jpg|left|200px]]
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-'''Crystal structure of the Non-desensitizing GluR2 ligand binding core mutant (S1S2J-L483Y) in complex with AMPA at 2.3 resolution'''
+===Crystal structure of the Non-desensitizing GluR2 ligand binding core mutant (S1S2J-L483Y) in complex with AMPA at 2.3 resolution===
-==Overview==
+<!--
-Ligand-gated ion channels transduce chemical signals into electrical impulses by opening a transmembrane pore in response to binding one or more neurotransmitter molecules. After activation, many ligand-gated ion channels enter a desensitized state in which the neurotransmitter remains bound but the ion channel is closed. Although receptor desensitization is crucial to the functioning of many ligand-gated ion channels in vivo, the molecular basis of this important process has until now defied analysis. Using the GluR2 AMPA-sensitive glutamate receptor, we show here that the ligand-binding cores form dimers and that stabilization of the intradimer interface by either mutations or allosteric modulators reduces desensitization. Perturbations that destabilize the interface enhance desensitization. Receptor activation involves conformational changes within each subunit that result in an increase in the separation of portions of the receptor that are linked to the ion channel. Our analysis defines the dimer interface in the resting and activated state, indicates how ligand binding is coupled to gating, and suggests modes of dimer dimer interaction in the assembled tetramer. Desensitization occurs through rearrangement of the dimer interface, which disengages the agonist-induced conformational change in the ligand-binding core from the ion channel gate.
+The line below this paragraph, {{ABSTRACT_PUBMED_12015593}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12015593 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12015593}}
 ==About this Structure==
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 [[Category: Point mutation]]
 [[Category: S1s2]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:44:47 2008''
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