3b6t

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[[Image:3b6t.jpg|left|200px]]
[[Image:3b6t.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 3b6t |SIZE=350|CAPTION= <scene name='initialview01'>3b6t</scene>, resolution 2.10&Aring;
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The line below this paragraph, containing "STRUCTURE_3b6t", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+901'>AC1</scene> and <scene name='pdbsite=AC2:Qus+Binding+Site+For+Residue+A+801'>AC2</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=QUS:(S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC+ACID'>QUS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= Gria2, Glur2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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-->
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|DOMAIN=
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{{STRUCTURE_3b6t| PDB=3b6t | SCENE= }}
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|RELATEDENTRY=[[1fto|1FTO]], [[1ftj|1FTJ]], [[1p1u|1P1U]], [[3b6q|3B6Q]], [[3b6w|3B6W]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b6t OCA], [http://www.ebi.ac.uk/pdbsum/3b6t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3b6t RCSB]</span>
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}}
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'''Crystal Structure of the GLUR2 Ligand Binding Core (S1S2J) T686A Mutant in Complex with Quisqualate at 2.1 Resolution'''
'''Crystal Structure of the GLUR2 Ligand Binding Core (S1S2J) T686A Mutant in Complex with Quisqualate at 2.1 Resolution'''
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[[Category: Howe, J R.]]
[[Category: Howe, J R.]]
[[Category: Lolis, E.]]
[[Category: Lolis, E.]]
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[[Category: alternative splicing]]
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[[Category: Alternative splicing]]
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[[Category: ampa receptor]]
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[[Category: Ampa receptor]]
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[[Category: cell junction]]
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[[Category: Cell junction]]
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[[Category: glur2]]
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[[Category: Glur2]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: ion transport]]
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[[Category: Ion transport]]
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[[Category: ionic channel]]
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[[Category: Ionic channel]]
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[[Category: ionotropic glutamate receptor]]
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[[Category: Ionotropic glutamate receptor]]
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[[Category: lipoprotein]]
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[[Category: Lipoprotein]]
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[[Category: membrane]]
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[[Category: Membrane]]
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[[Category: membrane protein]]
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[[Category: Membrane protein]]
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[[Category: mutant,quisqualate]]
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[[Category: Mutant,quisqualate]]
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[[Category: palmitate]]
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[[Category: Palmitate]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: postsynaptic cell membrane]]
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[[Category: Postsynaptic cell membrane]]
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[[Category: rna editing]]
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[[Category: Rna editing]]
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[[Category: synapse]]
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[[Category: Synapse]]
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[[Category: t686a]]
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[[Category: T686a]]
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[[Category: transmembrane]]
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[[Category: Transmembrane]]
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[[Category: transport]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:26:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:23:33 2008''
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Revision as of 17:26, 4 May 2008

Image:3b6t.jpg

Template:STRUCTURE 3b6t

Crystal Structure of the GLUR2 Ligand Binding Core (S1S2J) T686A Mutant in Complex with Quisqualate at 2.1 Resolution


Overview

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.

About this Structure

3B6T 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 Page seeded by OCA on Sun May 4 20:26:53 2008

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