6lu9

<table><tr><td colspan='2'>[[6lu9]] is a 4 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=6LU9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LU9 FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Grid2 ([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'>[http://proteopedia.org/fgij/fg.htm?mol=6lu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lu9 OCA], [http://pdbe.org/6lu9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lu9 RCSB], [http://www.ebi.ac.uk/pdbsum/6lu9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lu9 ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/GRID2_RAT GRID2_RAT]] Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists.

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== Publication Abstract from PubMed ==

GluD2 receptor belongs to the orphan delta family of glutamate receptor ion channels. These receptors play key roles in synaptogenesis and synaptic plasticity and are associated with multiple neuronal disorders like schizophrenia, autism spectrum disorder, cerebellar ataxia, intellectual disability, paraplegia, retinal dystrophy, etc. Despite the importance of these receptors in CNS, insights into full-length GluD2 receptor structure is missing till-date. Here we report cryo-electron microscopy structure of the rat GluD2 receptor in the presence of calcium ions and the ligand 7-chlorokynurenic acid, elucidating its 3D architecture. The structure reveals a non-swapped architecture at the extracellular amino-terminal (ATD), and ligand-binding domain (LBD) interface similar to that observed in GluD1; however, the organization and arrangement of the ATD and LBD domains in GluD2 are unique. While our results demonstrate that non-swapped architecture is conserved in the delta receptor family, they also highlight the differences that exist between the two member receptors; GluD1 and GluD2.

The architecture of GluD2 ionotropic delta glutamate receptor elucidated by cryo-EM.,Burada AP, Vinnakota R, Kumar J J Struct Biol. 2020 Aug 1;211(2):107546. doi: 10.1016/j.jsb.2020.107546. Epub, 2020 Jun 5. PMID:32512155<ref>PMID:32512155</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Buffalo rat]]

[[Category: Burada, A P]]

[[Category: Kumar, J]]

[[Category: Membrane protein]]