3oel

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<StructureSection load='3oel' size='340' side='right'caption='[[3oel]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3oel' size='340' side='right'caption='[[3oel]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3oel]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OEL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3oel]] is a 1 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=3OEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OEL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</scene></td></tr>
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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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3oek|3oek]], [[3oen|3oen]], [[3oem|3oem]]</div></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=DGL:D-GLUTAMIC+ACID'>DGL</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GluN2D, Grin2d ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
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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=3oel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oel OCA], [https://pdbe.org/3oel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oel RCSB], [https://www.ebi.ac.uk/pdbsum/3oel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oel ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oel OCA], [https://pdbe.org/3oel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oel RCSB], [https://www.ebi.ac.uk/pdbsum/3oel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oel ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/NMDE4_RAT NMDE4_RAT]] NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine.
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[https://www.uniprot.org/uniprot/NMDE4_RAT NMDE4_RAT] NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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N-methyl-D-aspartate (NMDA) receptors belong to the family of ionotropic glutamate receptors that mediate a majority of excitatory synaptic transmission. One unique property of GluN1/GluN2D NMDA receptors is an unusually prolonged deactivation time course following the removal of L-glutamate. Here we show, using x-ray crystallography and electrophysiology, that the deactivation time course of GluN1/GluN2D receptors is influenced by the conformational variability of the ligand-binding domain (LBD) as well as the structure of the activating ligand. L-glutamate and L-CCG-IV induce significantly slower deactivation time courses compared with other agonists. Crystal structures of the isolated GluN2D LBD in complex with various ligands reveal that the binding of L-glutamate induces a unique conformation at the backside of the ligand-binding site in proximity to the region at which the transmembrane domain would be located in the intact receptors. These data suggest that the activity of the GluN1/GluN2D NMDA receptor is controlled distinctively by the endogenous neurotransmitter L-glutamate.
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Ligand-specific deactivation time course of GluN1/GluN2D NMDA receptors.,Vance KM, Simorowski N, Traynelis SF, Furukawa H Nat Commun. 2011 Apr;2:294. PMID:21522138<ref>PMID:21522138</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 3oel" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Furukawa, H]]
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[[Category: Rattus norvegicus]]
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[[Category: Simorowski, N]]
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[[Category: Furukawa H]]
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[[Category: D-glutamate]]
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[[Category: Simorowski N]]
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[[Category: Disulfide bond]]
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[[Category: Ion channel]]
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[[Category: Transport protein]]
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Revision as of 11:16, 21 February 2024

Crystal structure of GluN2D ligand-binding core in complex with D-glutamate

PDB ID 3oel

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