View source for 6jfz


==GluK3 receptor complex with UBP310==
<SX load='6jfz' size='340' side='right' viewer='molstar' caption='[[6jfz]], [[Resolution|resolution]] 7.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jfz]] 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=6JFZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JFZ FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Grik3, Glur7 ([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=6jfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jfz OCA], [http://pdbe.org/6jfz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jfz RCSB], [http://www.ebi.ac.uk/pdbsum/6jfz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jfz ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/GRIK3_RAT GRIK3_RAT]] Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. 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. This receptor binds domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA.<ref>PMID:21907808</ref>  
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== Publication Abstract from PubMed ==
GluK3-kainate receptors are atypical members of the iGluR family that reside at both the pre- and postsynapse and play a vital role in the regulation of synaptic transmission. For a better understanding of structural changes that underlie receptor functions, GluK3 receptors were trapped in desensitized and resting/closed states and structures analyzed using single particle cryo-electron microscopy. While the desensitized GluK3 has domain organization as seen earlier for another kainate receptor-GluK2, antagonist bound GluK3 trapped a resting state with only two LBD domains in dimeric arrangement necessary for receptor activation. Using structures as a guide, we show that the N-linked glycans at the interface of GluK3 ATD and LBD likely mediate inter-domain interactions and attune receptor-gating properties. The mutational analysis also identified putative N-glycan interacting residues. Our results provide a molecular framework for understanding gating properties unique to GluK3 and exploring the role of N-linked glycosylation in their modulation.

Structural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery.,Kumari J, Vinnakota R, Kumar J Sci Rep. 2019 Jul 16;9(1):10254. doi: 10.1038/s41598-019-46770-z. PMID:31311973<ref>PMID:31311973</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6jfz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</SX>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Kumar, J]]
[[Category: Kumari, J]]
[[Category: Glutamate receptor]]
[[Category: Kainate]]
[[Category: Membrane protein]]
[[Category: Ubp310]]