3kg2

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[[Image:3kg2.png|left|200px]]
 
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==AMPA subtype ionotropic glutamate receptor in complex with competitive antagonist ZK 200775==
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The line below this paragraph, containing "STRUCTURE_3kg2", creates the "Structure Box" on the page.
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<StructureSection load='3kg2' size='340' side='right'caption='[[3kg2]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3kg2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KG2 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZK1:{[7-MORPHOLIN-4-YL-2,3-DIOXO-6-(TRIFLUOROMETHYL)-3,4-DIHYDROQUINOXALIN-1(2H)-YL]METHYL}PHOSPHONIC+ACID'>ZK1</scene></td></tr>
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{{STRUCTURE_3kg2| PDB=3kg2 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3kg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kg2 OCA], [https://pdbe.org/3kg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kg2 RCSB], [https://www.ebi.ac.uk/pdbsum/3kg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kg2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kg/3kg2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3kg2 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ionotropic glutamate receptors mediate most excitatory neurotransmission in the central nervous system and function by opening a transmembrane ion channel upon binding of glutamate. Despite their crucial role in neurobiology, the architecture and atomic structure of an intact ionotropic glutamate receptor are unknown. Here we report the crystal structure of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive, homotetrameric, rat GluA2 receptor at 3.6 A resolution in complex with a competitive antagonist. The receptor harbours an overall axis of two-fold symmetry with the extracellular domains organized as pairs of local dimers and with the ion channel domain exhibiting four-fold symmetry. A symmetry mismatch between the extracellular and ion channel domains is mediated by two pairs of conformationally distinct subunits, A/C and B/D. Therefore, the stereochemical manner in which the A/C subunits are coupled to the ion channel gate is different from the B/D subunits. Guided by the GluA2 structure and site-directed cysteine mutagenesis, we suggest that GluN1 and GluN2A NMDA (N-methyl-d-aspartate) receptors have a similar architecture, with subunits arranged in a 1-2-1-2 pattern. We exploit the GluA2 structure to develop mechanisms of ion channel activation, desensitization and inhibition by non-competitive antagonists and pore blockers.
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===AMPA subtype ionotropic glutamate receptor in complex with competitive antagonist ZK 200775===
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X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor.,Sobolevsky AI, Rosconi MP, Gouaux E Nature. 2009 Dec 10;462(7274):745-56. Epub . PMID:19946266<ref>PMID:19946266</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3kg2" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19946266 is the PubMed ID number.
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{{ABSTRACT_PUBMED_19946266}}
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==About this Structure==
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[[3kg2]] is a 4 chain structure of [[Glutamate receptor (GluA2)]] and [[Ionotropic Glutamate Receptors]] with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KG2 OCA].
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==See Also==
==See Also==
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*[[Anisotropic refinement|Anisotropic refinement]]
 
*[[Glutamate receptor (GluA2)|Glutamate receptor (GluA2)]]
*[[Glutamate receptor (GluA2)|Glutamate receptor (GluA2)]]
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*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
*[[Ionotropic Glutamate Receptors|Ionotropic Glutamate Receptors]]
*[[Ionotropic Glutamate Receptors|Ionotropic Glutamate Receptors]]
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*[[Molecular Playground/Glutamate Receptor|Molecular Playground/Glutamate Receptor]]
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*[[Ionotropic receptors|Ionotropic receptors]]
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*[[Urea transporter|Urea transporter]]
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*[[Ligand-gated ion channels (ionotropic receptors)|Ligand-gated ion channels (ionotropic receptors)]]
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*[[User:Wayne Decatur|User:Wayne Decatur]]
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== References ==
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*[[User:Wayne Decatur/3kg2 Morph Methods|User:Wayne Decatur/3kg2 Morph Methods]]
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:019946266</ref><references group="xtra"/>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Gouaux, E.]]
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[[Category: Gouaux E]]
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[[Category: Rosconi, M P.]]
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[[Category: Rosconi MP]]
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[[Category: Sobolevsky, A I.]]
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[[Category: Sobolevsky AI]]
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[[Category: Cell membrane]]
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[[Category: Glycoprotein]]
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[[Category: Ion channel]]
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[[Category: Ion transport]]
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[[Category: Membrane]]
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[[Category: Membrane protein]]
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[[Category: Postsynaptic cell membrane]]
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[[Category: Receptor]]
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[[Category: Rna editing]]
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[[Category: Synapse]]
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[[Category: Tetramer]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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[[Category: Transport protein]]
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Current revision

AMPA subtype ionotropic glutamate receptor in complex with competitive antagonist ZK 200775

PDB ID 3kg2

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