6fqj: Difference between revisions

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New page: '''Unreleased structure''' The entry 6fqj is ON HOLD until Paper Publication Authors: Coombs, I.D., Soto, D., Gold, M.G., Farrant, M.F., Cull-Candy, S.G. Description: GluA2(flop) G724C...
 
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'''Unreleased structure'''


The entry 6fqj is ON HOLD until Paper Publication
==GluA2(flop) G724C ligand binding core dimer bound to ZK200775 at 2.50 Angstrom resolution==
<StructureSection load='6fqj' size='340' side='right'caption='[[6fqj]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fqj]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FQJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FQJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZK1:{[7-MORPHOLIN-4-YL-2,3-DIOXO-6-(TRIFLUOROMETHYL)-3,4-DIHYDROQUINOXALIN-1(2H)-YL]METHYL}PHOSPHONIC+ACID'>ZK1</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Gria2, Glur2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fqj OCA], [http://pdbe.org/6fqj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fqj RCSB], [http://www.ebi.ac.uk/pdbsum/6fqj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fqj ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/GRIA2_RAT GRIA2_RAT]] Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. 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. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.<ref>PMID:9351977</ref> <ref>PMID:19265014</ref> <ref>PMID:21172611</ref> <ref>PMID:12501192</ref> <ref>PMID:12015593</ref> <ref>PMID:12872125</ref> <ref>PMID:12730367</ref> <ref>PMID:16192394</ref> <ref>PMID:15591246</ref> <ref>PMID:17018279</ref> <ref>PMID:16483599</ref> <ref>PMID:19946266</ref> <ref>PMID:21317873</ref> <ref>PMID:21846932</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Desensitization is a canonical property of ligand-gated ion channels, causing progressive current decline in the continued presence of agonist. AMPA-type glutamate receptors (AMPARs), which mediate fast excitatory signaling throughout the brain, exhibit profound desensitization. Recent cryo-EM studies of AMPAR assemblies show their ion channels to be closed in the desensitized state. Here we present evidence that homomeric Q/R-edited AMPARs still allow ions to flow when the receptors are desensitized. GluA2(R) expressed alone, or with auxiliary subunits (gamma-2, gamma-8 or GSG1L), generates large fractional steady-state currents and anomalous current-variance relationships. Our results from fluctuation analysis, single-channel recording, and kinetic modeling, suggest that the steady-state current is mediated predominantly by conducting desensitized receptors. When combined with crystallography this unique functional readout of a hitherto silent state enabled us to examine cross-linked cysteine mutants to probe the conformation of the desensitized ligand binding domain of functioning AMPAR complexes.


Authors: Coombs, I.D., Soto, D., Gold, M.G., Farrant, M.F., Cull-Candy, S.G.
Homomeric GluA2(R) AMPA receptors can conduct when desensitized.,Coombs ID, Soto D, McGee TP, Gold MG, Farrant M, Cull-Candy SG Nat Commun. 2019 Sep 20;10(1):4312. doi: 10.1038/s41467-019-12280-9. PMID:31541113<ref>PMID:31541113</ref>


Description: GluA2(flop) G724C ligand binding core dimer bound to ZK200775 at 2.50 Angstrom resolution
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Gold, M.G]]
<div class="pdbe-citations 6fqj" style="background-color:#fffaf0;"></div>
[[Category: Cull-Candy, S.G]]
 
[[Category: Farrant, M.F]]
==See Also==
*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Coombs, I D]]
[[Category: Cull-Candy, S G]]
[[Category: Farrant, M F]]
[[Category: Gold, M G]]
[[Category: Soto, D]]
[[Category: Soto, D]]
[[Category: Coombs, I.D]]
[[Category: Ampar receptor]]
[[Category: Competitive antagonist]]
[[Category: Cross-linked dimer]]
[[Category: Ligand binding domain]]
[[Category: Membrane protein]]
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