View source for 6mmp


==Diheteromeric NMDA receptor GluN1/GluN2A in the '2-Knuckle-Symmetric' conformation, in complex with glycine and glutamate, in the presence of 0.1 millimolar EDTA, and at pH 8.0==
<SX load='6mmp' size='340' side='right' viewer='molstar' caption='[[6mmp]], [[Resolution|resolution]] 6.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6mmp]] is a 4 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=6MMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MMP 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]] 6.88&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=6mmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mmp OCA], [https://pdbe.org/6mmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mmp RCSB], [https://www.ebi.ac.uk/pdbsum/6mmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mmp ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
N-methyl-D-aspartate receptors (NMDARs) play essential roles in memory formation, neuronal plasticity, and brain development, with their dysfunction linked to a range of disorders from ischemia to schizophrenia. Zinc and pH are physiological allosteric modulators of NMDARs, with GluN2A-containing receptors inhibited by nanomolar concentrations of divalent zinc and by excursions to low pH. Despite the widespread importance of zinc and proton modulation of NMDARs, the molecular mechanism by which these ions modulate receptor activity has proven elusive. Here, we use cryoelectron microscopy to elucidate the structure of the GluN1/GluN2A NMDAR in a large ensemble of conformations under a range of physiologically relevant zinc and proton concentrations. We show how zinc binding to the amino terminal domain elicits structural changes that are transduced though the ligand-binding domain and result in constriction of the ion channel gate.

Mechanisms for Zinc and Proton Inhibition of the GluN1/GluN2A NMDA Receptor.,Jalali-Yazdi F, Chowdhury S, Yoshioka C, Gouaux E Cell. 2018 Nov 29;175(6):1520-1532.e15. doi: 10.1016/j.cell.2018.10.043. PMID:30500536<ref>PMID:30500536</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6mmp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Chowdhury S]]
[[Category: Gouaux E]]
[[Category: Jalali-Yazdi F]]
[[Category: Yoshioka C]]