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| <StructureSection load='7ryy' size='340' side='right'caption='[[7ryy]], [[Resolution|resolution]] 4.40Å' scene=''> | | <StructureSection load='7ryy' size='340' side='right'caption='[[7ryy]], [[Resolution|resolution]] 4.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7ryy]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RYY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RYY FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RYY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RYY FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.4Å</td></tr> |
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</scene></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=7ryy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ryy OCA], [https://pdbe.org/7ryy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ryy RCSB], [https://www.ebi.ac.uk/pdbsum/7ryy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ryy ProSAT]</span></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=7ryy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ryy OCA], [https://pdbe.org/7ryy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ryy RCSB], [https://www.ebi.ac.uk/pdbsum/7ryy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ryy ProSAT]</span></td></tr> |
| </table> | | </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>
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| AMPA receptors (AMPARs) mediate the majority of excitatory neurotransmission. Their surface expression, trafficking, gating, and pharmacology are regulated by auxiliary subunits. Of the two types of TARP auxiliary subunits, type I TARPs assume activating roles, while type II TARPs serve suppressive functions. We present cryo-EM structures of GluA2 AMPAR in complex with type II TARP gamma5, which reduces steady-state currents, increases single-channel conductance, and slows recovery from desensitization. Regulation of AMPAR function depends on its ligand-binding domain (LBD) interaction with the gamma5 head domain. GluA2-gamma5 complex shows maximum stoichiometry of two TARPs per AMPAR tetramer, being different from type I TARPs but reminiscent of the auxiliary subunit GSG1L. Desensitization of both GluA2-GSG1L and GluA2-gamma5 complexes is accompanied by rupture of LBD dimer interface, while GluA2-gamma5 but not GluA2-GSG1L LBD dimers remain two-fold symmetric. Different structural architectures and desensitization mechanisms of complexes with auxiliary subunits endow AMPARs with broad functional capabilities.
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| Structure and desensitization of AMPA receptor complexes with type II TARP gamma5 and GSG1L.,Klykov O, Gangwar SP, Yelshanskaya MV, Yen L, Sobolevsky AI Mol Cell. 2021 Dec 2;81(23):4771-4783.e7. doi: 10.1016/j.molcel.2021.09.030. Epub, 2021 Oct 21. PMID:34678168<ref>PMID:34678168</ref>
| | ==See Also== |
| | | *[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7ryy" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Gangwar, S P]] | | [[Category: Gangwar SP]] |
| [[Category: Klykov, O V]] | | [[Category: Klykov OV]] |
| [[Category: Sobolevsky, A I]] | | [[Category: Sobolevsky AI]] |
| [[Category: Yelshanskaya, M V]] | | [[Category: Yelshanskaya MV]] |
| [[Category: Ampa receptor]]
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| [[Category: Ion channel]]
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| [[Category: Membrane protein]]
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| [[Category: Neurotransmission]]
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| [[Category: Synapse]]
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| [[Category: Tarp gamma-5]]
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