5ict: Difference between revisions

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-'''Unreleased structure'''
-The entry 5ict is ON HOLD  until Paper Publication
+==Crystal structure of the Drosophila GluR1A ligand binding domain Y792T mutant complex with glutamate==
+<StructureSection load='5ict' size='340' side='right' caption='[[5ict]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ict]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ICT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ICT FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5ict FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ict OCA], [http://pdbe.org/5ict PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ict RCSB], [http://www.ebi.ac.uk/pdbsum/5ict PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ict ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/GLR1_DROME GLR1_DROME]] 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 (By similarity). Forms ligand-gated ion channels which are activated by kainate.<ref>PMID:1359540</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Phylogenetic analysis reveals AMPA, kainate, and NMDA receptor families in insect genomes, suggesting conserved functional properties corresponding to their vertebrate counterparts. However, heterologous expression of the Drosophila kainate receptor DKaiR1D and the AMPA receptor DGluR1A revealed novel ligand selectivity at odds with the classification used for vertebrate glutamate receptor ion channels (iGluRs). DKaiR1D forms a rapidly activating and desensitizing receptor that is inhibited by both NMDA and the NMDA receptor antagonist AP5; crystallization of the KaiR1D ligand-binding domain reveals that these ligands stabilize open cleft conformations, explaining their action as antagonists. Surprisingly, the AMPA receptor DGluR1A shows weak activation by its namesake agonist AMPA and also by quisqualate. Crystallization of the DGluR1A ligand-binding domain reveals amino acid exchanges that interfere with binding of these ligands. The unexpected ligand-binding profiles of insect iGluRs allows classical tools to be used in novel approaches for the study of synaptic regulation. VIDEO ABSTRACT.
-Authors:
+Novel Functional Properties of Drosophila CNS Glutamate Receptors.,Li Y, Dharkar P, Han TH, Serpe M, Lee CH, Mayer ML Neuron. 2016 Dec 7;92(5):1036-1048. doi: 10.1016/j.neuron.2016.10.058. Epub 2016 , Nov 23. PMID:27889096<ref>PMID:27889096</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5ict" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Dharkar, P]]
+[[Category: Mayer, M L]]
+[[Category: Membrane protein]]