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3h5v
From Proteopedia
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| - | [[Image:3h5v.png|left|200px]] | ||
| - | + | ==Crystal structure of the GluR2-ATD== | |
| + | <StructureSection load='3h5v' size='340' side='right'caption='[[3h5v]], [[Resolution|resolution]] 2.33Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3h5v]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H5V FirstGlance]. <br> | ||
| + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3h5w|3h5w]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Gria2, Glur2 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3h5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h5v OCA], [https://pdbe.org/3h5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h5v RCSB], [https://www.ebi.ac.uk/pdbsum/3h5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h5v ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/GRIA2_RAT GRIA2_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. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.<ref>PMID:9351977</ref> <ref>PMID:19265014</ref> <ref>PMID:21172611</ref> <ref>PMID:12501192</ref> <ref>PMID:12015593</ref> <ref>PMID:12872125</ref> <ref>PMID:12730367</ref> <ref>PMID:16192394</ref> <ref>PMID:15591246</ref> <ref>PMID:17018279</ref> <ref>PMID:16483599</ref> <ref>PMID:19946266</ref> <ref>PMID:21317873</ref> <ref>PMID:21846932</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h5/3h5v_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3h5v ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fast excitatory neurotransmission is mediated largely by ionotropic glutamate receptors (iGluRs), tetrameric, ligand-gated ion channel proteins comprised of three subfamilies, AMPA, kainate and NMDA receptors, with each subfamily sharing a common, modular-domain architecture. For all receptor subfamilies, active channels are exclusively formed by assemblages of subunits within the same subfamily, a molecular process principally encoded by the amino-terminal domain (ATD). However, the molecular basis by which the ATD guides subfamily-specific receptor assembly is not known. Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers and, by the analysis of crystal structures of the GluR2-ATD, propose mechanisms by which the ATD guides subfamily-specific receptor assembly. | ||
| - | + | Crystal structure and association behaviour of the GluR2 amino-terminal domain.,Jin R, Singh SK, Gu S, Furukawa H, Sobolevsky AI, Zhou J, Jin Y, Gouaux E EMBO J. 2009 Jun 17;28(12):1812-23. Epub 2009 May 21. PMID:19461580<ref>PMID:19461580</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3h5v" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[ | + | *[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Furukawa, H | + | [[Category: Buffalo rat]] |
| - | [[Category: Gouaux, E | + | [[Category: Large Structures]] |
| - | [[Category: Gu, S | + | [[Category: Furukawa, H]] |
| - | [[Category: Jin, R | + | [[Category: Gouaux, E]] |
| - | [[Category: Jin, Y | + | [[Category: Gu, S]] |
| - | [[Category: Singh, S K | + | [[Category: Jin, R]] |
| - | [[Category: Sobolevsky, A | + | [[Category: Jin, Y]] |
| - | [[Category: Zhou, J | + | [[Category: Singh, S K]] |
| + | [[Category: Sobolevsky, A]] | ||
| + | [[Category: Zhou, J]] | ||
[[Category: Cell junction]] | [[Category: Cell junction]] | ||
[[Category: Cell membrane]] | [[Category: Cell membrane]] | ||
Current revision
Crystal structure of the GluR2-ATD
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Categories: Buffalo rat | Large Structures | Furukawa, H | Gouaux, E | Gu, S | Jin, R | Jin, Y | Singh, S K | Sobolevsky, A | Zhou, J | Cell junction | Cell membrane | Endoplasmic reticulum | Glutamate receptor | Glycoprotein | Ion transport | Ionic channel | Ligand-gated ion channel | Lipoprotein | Membrane | Palmitate | Phosphoprotein | Postsynaptic cell membrane | Receptor | Rna editing | Synapse | Transmembrane | Transport | Transport protein

