3oen: Difference between revisions
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==Crystal structure of GluN2D ligand-binding core in complex with L-glutamate== | |||
=== | <StructureSection load='3oen' size='340' side='right' caption='[[3oen]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3oen]] is a 1 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=3OEN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OEN FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3oek|3oek]], [[3oel|3oel]], [[3oem|3oem]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GluN2D, Grin2d ([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=3oen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oen OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oen RCSB], [http://www.ebi.ac.uk/pdbsum/3oen PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
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: Furukawa, H | [[Category: Furukawa, H]] | ||
[[Category: Simorowski, N | [[Category: Simorowski, N]] | ||
[[Category: Disulfide bond]] | [[Category: Disulfide bond]] | ||
[[Category: Ion channel]] | [[Category: Ion channel]] | ||
[[Category: L-glutamate]] | [[Category: L-glutamate]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
Revision as of 06:38, 19 December 2014
Crystal structure of GluN2D ligand-binding core in complex with L-glutamate
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