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| | ==Crystal structure of GluN2D ligand-binding core in complex with N-methyl-D-aspartate== | | ==Crystal structure of GluN2D ligand-binding core in complex with N-methyl-D-aspartate== |
| - | <StructureSection load='3oem' size='340' side='right' caption='[[3oem]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='3oem' size='340' side='right'caption='[[3oem]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3oem]] is a 1 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=3OEM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OEM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3oem]] 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=3OEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OEM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OEM:N-METHYL-D-ASPARTIC+ACID'>OEM</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3oek|3oek]], [[3oel|3oel]], [[3oen|3oen]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OEM:N-METHYL-D-ASPARTIC+ACID'>OEM</scene></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 Buffalo rat])</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=3oem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oem OCA], [https://pdbe.org/3oem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oem RCSB], [https://www.ebi.ac.uk/pdbsum/3oem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oem ProSAT]</span></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=3oem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oem OCA], [http://pdbe.org/3oem PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3oem RCSB], [http://www.ebi.ac.uk/pdbsum/3oem PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3oem ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| - | <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.
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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>
| + | ==See Also== |
| - | | + | *[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3oem" style="background-color:#fffaf0;"></div>
| + | |
| - | == References == | + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Large Structures]] |
| - | [[Category: Furukawa, H]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Simorowski, N]] | + | [[Category: Furukawa H]] |
| - | [[Category: Ion channel]]
| + | [[Category: Simorowski N]] |
| - | [[Category: N-methyl-d-aspartate]] | + | |
| - | [[Category: Transport protein]]
| + | |
