2i3v

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[[Image:2i3v.gif|left|200px]]
 
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{{Structure
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==Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant==
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|PDB= 2i3v |SIZE=350|CAPTION= <scene name='initialview01'>2i3v</scene>, resolution 2.40&Aring;
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<StructureSection load='2i3v' size='340' side='right'caption='[[2i3v]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[2i3v]] 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=2I3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I3V FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.4&#8491;</td></tr>
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|GENE= Gria2, Glur2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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<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=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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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=2i3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i3v OCA], [https://pdbe.org/2i3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i3v RCSB], [https://www.ebi.ac.uk/pdbsum/2i3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i3v ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1ftj|1FTJ]], [[2i3w|2I3W]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i3v OCA], [http://www.ebi.ac.uk/pdbsum/2i3v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i3v RCSB]</span>
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== Function ==
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}}
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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/i3/2i3v_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=2i3v 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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The canonical conformational states occupied by most ligand-gated ion channels, and many cell-surface receptors, are the resting, activated, and desensitized states. While the resting and activated states of multiple receptors are well characterized, elaboration of the structural properties of the desensitized state, a state that is by definition inactive, has proven difficult. Here we use electrical, chemical, and crystallographic experiments on the AMPA-sensitive GluR2 receptor, defining the conformational rearrangements of the agonist binding cores that occur upon desensitization of this ligand-gated ion channel. These studies demonstrate that desensitization involves the rupture of an extensive interface between domain 1 of 2-fold related glutamate-binding core subunits, compensating for the ca. 21 degrees of domain closure induced by glutamate binding. The rupture of the domain 1 interface allows the ion channel to close and thereby provides a simple explanation to the long-standing question of how agonist binding is decoupled from ion channel gating upon receptor desensitization.
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'''Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant'''
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Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor.,Armstrong N, Jasti J, Beich-Frandsen M, Gouaux E Cell. 2006 Oct 6;127(1):85-97. PMID:17018279<ref>PMID:17018279</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>
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<div class="pdbe-citations 2i3v" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The canonical conformational states occupied by most ligand-gated ion channels, and many cell-surface receptors, are the resting, activated, and desensitized states. While the resting and activated states of multiple receptors are well characterized, elaboration of the structural properties of the desensitized state, a state that is by definition inactive, has proven difficult. Here we use electrical, chemical, and crystallographic experiments on the AMPA-sensitive GluR2 receptor, defining the conformational rearrangements of the agonist binding cores that occur upon desensitization of this ligand-gated ion channel. These studies demonstrate that desensitization involves the rupture of an extensive interface between domain 1 of 2-fold related glutamate-binding core subunits, compensating for the ca. 21 degrees of domain closure induced by glutamate binding. The rupture of the domain 1 interface allows the ion channel to close and thereby provides a simple explanation to the long-standing question of how agonist binding is decoupled from ion channel gating upon receptor desensitization.
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*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2I3V is a [[Single protein]] structure of 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=2I3V OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor., Armstrong N, Jasti J, Beich-Frandsen M, Gouaux E, Cell. 2006 Oct 6;127(1):85-97. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17018279 17018279]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Armstrong N]]
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[[Category: Armstrong, N.]]
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[[Category: Beich-Frandsen M]]
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[[Category: Beich-Frandsen, M.]]
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[[Category: Gouaux E]]
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[[Category: Gouaux, E.]]
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[[Category: Jasti J]]
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[[Category: Jasti, J.]]
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[[Category: ionotropic glutamate receptor ligand binding core s1s2 g725c mutant]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:39:18 2008''
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Current revision

Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant

PDB ID 2i3v

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