3g3h

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{{Seed}}
 
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[[Image:3g3h.jpg|left|200px]]
 
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==Crystal structure of the GluR6 ligand binding domain dimer K665R I749L Q753K mutant with glutamate and NaCl at 1.5 Angstrom resolution==
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The line below this paragraph, containing "STRUCTURE_3g3h", creates the "Structure Box" on the page.
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<StructureSection load='3g3h' size='340' side='right'caption='[[3g3h]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3g3h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G3H FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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{{STRUCTURE_3g3h| PDB=3g3h | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3g3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g3h OCA], [https://pdbe.org/3g3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g3h RCSB], [https://www.ebi.ac.uk/pdbsum/3g3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g3h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GRIK2_RAT GRIK2_RAT] Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus. Modulates cell surface expression of NETO2 (By similarity).<ref>PMID:17486098</ref> <ref>PMID:17115050</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g3/3g3h_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3g3h ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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AMPA and kainate receptors mediate fast synaptic transmission. AMPA receptor ligand-binding domains form dimers, which are key functional units controlling ion-channel activation and desensitization. Dimer stability is inversely related to the rate and extent of desensitization. Kainate and AMPA receptors share common structural elements, but functional measurements suggest that subunit assembly and gating differs between these subtypes. To investigate this, we constructed a library of GluR6 kainate receptor mutants and directly measured changes in kainate receptor dimer stability by analytical ultracentrifugation, which, combined with electrophysiological experiments, revealed an inverse correlation between dimer stability and the rate of desensitization. We solved crystal structures for a series of five GluR6 mutants, to understand the molecular mechanisms for dimer stabilization. We demonstrate that the desensitized state of kainate receptors acts as a deep energy well offsetting the stabilizing effects of dimer interface mutants, and that the deactivation of kainate receptor responses is dominated by entry into desensitized states. Our results show how neurotransmitter receptors with similar structures and gating mechanisms can exhibit strikingly different functional properties.
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===Crystal structure of the GluR6 ligand binding domain dimer K665R I749L Q753K mutant with glutamate and NaCl at 1.5 Angstrom resolution===
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Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization.,Chaudhry C, Weston MC, Schuck P, Rosenmund C, Mayer ML EMBO J. 2009 May 20;28(10):1518-30. Epub 2009 Apr 2. PMID:19339989<ref>PMID:19339989</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3g3h" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19339989}}, adds the Publication Abstract to the page
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*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19339989 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19339989}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3G3H is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G3H OCA].
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==Reference==
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<ref group="xtra">PMID:19339989</ref><references group="xtra"/>
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Chaudhry, C.]]
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[[Category: Chaudhry C]]
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[[Category: Mayer, M L.]]
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[[Category: Mayer ML]]
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[[Category: Cell junction]]
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[[Category: Cell membrane]]
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[[Category: Glycoprotein]]
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[[Category: Ion transport]]
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[[Category: Ionic channel]]
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[[Category: Membrane]]
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[[Category: Membrane protein]]
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[[Category: Postsynaptic cell membrane]]
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[[Category: Receptor]]
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[[Category: Rna editing]]
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[[Category: Synapse]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 4 07:25:18 2009''
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Current revision

Crystal structure of the GluR6 ligand binding domain dimer K665R I749L Q753K mutant with glutamate and NaCl at 1.5 Angstrom resolution

PDB ID 3g3h

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