3b6q

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{{STRUCTURE_3b6q| PDB=3b6q | SCENE= }}
{{STRUCTURE_3b6q| PDB=3b6q | SCENE= }}
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'''Crystal Structure of the GLUR2 Ligand Binding Core (S1S2J) Mutant T686A in Complex with Glutamate at 2.0 Resolution'''
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===Crystal Structure of the GLUR2 Ligand Binding Core (S1S2J) Mutant T686A in Complex with Glutamate at 2.0 Resolution===
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==Overview==
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At most excitatory central synapses, glutamate is released from presynaptic terminals and binds to postsynaptic AMPA receptors, initiating a series of conformational changes that result in ion channel opening. Efficient transmission at these synapses requires that glutamate binding to AMPA receptors results in rapid and near-synchronous opening of postsynaptic receptor channels. In addition, if the information encoded in the frequency of action potential discharge is to be transmitted faithfully, glutamate must dissociate from the receptor quickly, enabling the synapse to discriminate presynaptic action potentials that are spaced closely in time. The current view is that the efficacy of agonists is directly related to the extent to which ligand binding results in closure of the binding domain. For glutamate to dissociate from the receptor, however, the binding domain must open. Previously, we showed that mutations in glutamate receptor subunit 2 that should destabilize the closed conformation not only sped deactivation but also altered the relative efficacy of glutamate and quisqualate. Here we present x-ray crystallographic and single-channel data that support the conclusions that binding domain closing necessarily precedes channel opening and that the kinetics of conformational changes at the level of the binding domain importantly influence ion channel gating. Our findings suggest that the stability of the closed-cleft conformation has been tuned during evolution so that glutamate dissociates from the receptor as rapidly as possible but remains an efficacious agonist.
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(as it appears on PubMed at http://www.pubmed.gov), where 18216201 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18216201}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural and single-channel results indicate that the rates of ligand binding domain closing and opening directly impact AMPA receptor gating., Zhang W, Cho Y, Lolis E, Howe JR, J Neurosci. 2008 Jan 23;28(4):932-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18216201 18216201]
Structural and single-channel results indicate that the rates of ligand binding domain closing and opening directly impact AMPA receptor gating., Zhang W, Cho Y, Lolis E, Howe JR, J Neurosci. 2008 Jan 23;28(4):932-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18216201 18216201]
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Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes., Armstrong N, Mayer M, Gouaux E, Proc Natl Acad Sci U S A. 2003 May 13;100(10):5736-41. Epub 2003 May 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12730367 12730367]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Transmembrane]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:26:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:35:30 2008''

Revision as of 03:35, 28 July 2008

Image:3b6q.png

Template:STRUCTURE 3b6q

Crystal Structure of the GLUR2 Ligand Binding Core (S1S2J) Mutant T686A in Complex with Glutamate at 2.0 Resolution

Template:ABSTRACT PUBMED 18216201

About this Structure

3B6Q is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structural and single-channel results indicate that the rates of ligand binding domain closing and opening directly impact AMPA receptor gating., Zhang W, Cho Y, Lolis E, Howe JR, J Neurosci. 2008 Jan 23;28(4):932-43. PMID:18216201

Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes., Armstrong N, Mayer M, Gouaux E, Proc Natl Acad Sci U S A. 2003 May 13;100(10):5736-41. Epub 2003 May 2. PMID:12730367

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