3u94
From Proteopedia
(Difference between revisions)
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- | [[ | + | ==Crystal structure of the GluK3 ligand binding domain complex with glutamate and zinc: P21212 form== |
+ | <StructureSection load='3u94' size='340' side='right' caption='[[3u94]], [[Resolution|resolution]] 1.96Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3u94]] is a 4 chain structure with sequence 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=3U94 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U94 FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u92|3u92]], [[3u93|3u93]], [[3s9e|3s9e]], [[1s50|1s50]], [[1txf|1txf]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRIK3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</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=3u94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u94 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u94 RCSB], [http://www.ebi.ac.uk/pdbsum/3u94 PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Kainate receptors (KARs) play a key role in the regulation of synaptic networks. Here, we show that zinc, a cation released at a subset of glutamatergic synapses, potentiates glutamate currents mediated by homomeric and heteromeric KARs containing GluK3 at 10-100 muM concentrations, whereas it inhibits other KAR subtypes. Potentiation of GluK3 currents is mainly due to reduced desensitization, as shown by kinetic analysis and desensitization mutants. Crystallographic and mutation analyses revealed that a specific zinc binding site is formed at the base of the ligand binding domain (LBD) dimer interface by a GluK3-specific aspartate (Asp759), together with two conserved residues, His762 and Asp730, the latter located on the partner subunit. In addition, we propose that tetrameric GluK2/GluK3 receptors are likely assembled as pairs of heterodimeric LBDs. Therefore, zinc binding stabilizes the labile GluK3 dimer interface, slows desensitization, and potentiates currents, providing a mechanism for KAR potentiation at glutamatergic synapses. | ||
- | + | Zinc Potentiates GluK3 Glutamate Receptor Function by Stabilizing the Ligand Binding Domain Dimer Interface.,Veran J, Kumar J, Pinheiro PS, Athane A, Mayer ML, Perrais D, Mulle C Neuron. 2012 Nov 8;76(3):565-78. doi: 10.1016/j.neuron.2012.08.027. PMID:23141068<ref>PMID:23141068</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
- | + | ==See Also== | |
- | + | *[[Ionotropic Glutamate Receptors|Ionotropic Glutamate Receptors]] | |
- | == | + | == References == |
- | [[ | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
- | [[Category: Kumar, J | + | [[Category: Kumar, J]] |
- | [[Category: Mayer, M L | + | [[Category: Mayer, M L]] |
[[Category: Ion channel]] | [[Category: Ion channel]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] |
Revision as of 16:25, 9 December 2014
Crystal structure of the GluK3 ligand binding domain complex with glutamate and zinc: P21212 form
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