View source for 5ipr


==Cryo-EM structure of GluN1/GluN2B NMDA receptor in the DCKA/D-APV-bound conformation, state 3==
<StructureSection load='5ipr' size='340' side='right' caption='[[5ipr]], [[Resolution|resolution]] 14.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ipr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IPR FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5iou|5iou]], [[5iov|5iov]], [[5ipq|5ipq]], [[5ips|5ips]], [[5ipt|5ipt]], [[5ipu|5ipu]], [[5ipv|5ipv]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NR2B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog])</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=5ipr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ipr OCA], [http://pdbe.org/5ipr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ipr RCSB], [http://www.ebi.ac.uk/pdbsum/5ipr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ipr ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
N-methyl-D-aspartate receptors (NMDARs) are glutamate-gated, calcium-permeable ion channels that mediate synaptic transmission and underpin learning and memory. NMDAR dysfunction is directly implicated in diseases ranging from seizure to ischemia. Despite its fundamental importance, little is known about how the NMDAR transitions between inactive and active states and how small molecules inhibit or activate ion channel gating. Here, we report electron cryo-microscopy structures of the GluN1-GluN2B NMDA receptor in an ensemble of competitive antagonist-bound states, an agonist-bound form, and a state bound with agonists and the allosteric inhibitor Ro25-6981. Together with double electron-electron resonance experiments, we show how competitive antagonists rupture the ligand binding domain (LBD) gating "ring," how agonists retain the ring in a dimer-of-dimers configuration, and how allosteric inhibitors, acting within the amino terminal domain, further stabilize the LBD layer. These studies illuminate how the LBD gating ring is fundamental to signal transduction and gating in NMDARs.

Mechanism of NMDA Receptor Inhibition and Activation.,Zhu S, Stein RA, Yoshioka C, Lee CH, Goehring A, Mchaourab HS, Gouaux E Cell. 2016 Apr 21;165(3):704-14. doi: 10.1016/j.cell.2016.03.028. Epub 2016 Apr, 7. PMID:27062927<ref>PMID:27062927</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ipr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: African clawed frog]]
[[Category: Goehring, A]]
[[Category: Gouaux, E]]
[[Category: Lee, C H]]
[[Category: Mchaourab, S H]]
[[Category: Stein, A R]]
[[Category: Yoshioka, C]]
[[Category: Zhu, S]]
[[Category: Ligand-gated ion channel]]
[[Category: Signaling protein]]
[[Category: Synaptic transmission]]