View source for 7eou


==Structure of the human GluN1/GluN2A NMDA receptor in the glycine/glutamate/GNE-6901/9-AA bound state==
<StructureSection load='7eou' size='340' side='right'caption='[[7eou]], [[Resolution|resolution]] 4.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7eou]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EOU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6RM:7-[(4-FLUORANYLPHENOXY)METHYL]-3-[(1~{R},2~{R})-2-(HYDROXYMETHYL)CYCLOPROPYL]-2-METHYL-[1,3]THIAZOLO[3,2-A]PYRIMIDIN-5-ONE'>6RM</scene>, <scene name='pdbligand=AA:9-AMINOACRIDINE'>AA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=7eou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eou OCA], [https://pdbe.org/7eou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eou RCSB], [https://www.ebi.ac.uk/pdbsum/7eou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eou ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
N-methyl-D-aspartate (NMDA) receptors are glutamate-gated calcium-permeable ion channels that are widely implicated in synaptic transmission and plasticity. Here, we report a gallery of cryo-electron microscopy (cryo-EM) structures of the human GluN1-GluN2A NMDA receptor at an overall resolution of 4 A in complex with distinct ligands or modulators. In the full-length context of GluN1-GluN2A receptors, we visualize the competitive antagonists bound to the ligand-binding domains (LBDs) of GluN1 and GluN2A subunits, respectively. We reveal that the binding of positive allosteric modulator shortens the distance between LBDs and the transmembrane domain (TMD), which further stretches the opening of the gate. In addition, we unexpectedly visualize the binding cavity of the "foot-in-the-door" blocker 9-aminoacridine within the LBD-TMD linker region, differing from the conventional "trapping" blocker binding site at the vestibule within the TMD. Our study provides molecular insights into the crosstalk between LBDs and TMD during channel activation, inhibition, and allosteric transition.

Gating mechanism and a modulatory niche of human GluN1-GluN2A NMDA receptors.,Wang H, Lv S, Stroebel D, Zhang J, Pan Y, Huang X, Zhang X, Paoletti P, Zhu S Neuron. 2021 Aug 4;109(15):2443-2456.e5. doi: 10.1016/j.neuron.2021.05.031. Epub , 2021 Jun 28. PMID:34186027<ref>PMID:34186027</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7eou" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Wang H]]
[[Category: Zhu S]]