2i3w: Difference between revisions

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-[[Image:2i3w.gif|left|200px]]<br /><applet load="2i3w" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2i3w, resolution 2.30&Aring;" />
-'''Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of S729C mutant'''<br />
-==Overview==
+==Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of S729C mutant==
-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.
+<StructureSection load='2i3w' size='340' side='right'caption='[[2i3w]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2i3w]] is a 2 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=2I3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I3W FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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></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=2i3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i3w OCA], [https://pdbe.org/2i3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i3w RCSB], [https://www.ebi.ac.uk/pdbsum/2i3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i3w 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/i3/2i3w_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=2i3w ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==About this Structure==
+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>
-I3W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with GLU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2I3W OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17018279 17018279]
+</div>
+<div class="pdbe-citations 2i3w" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Armstrong N]]
-[[Category: Armstrong, N.]]
+[[Category: Beich-Frandsen M]]
-[[Category: Beich-Frandsen, M.]]
+[[Category: Gouaux E]]
-[[Category: Gouaux, E.]]
+[[Category: Jasti J]]
-[[Category: Jasti, J.]]
-[[Category: GLU]]
-[[Category: ionotropic glutamate receptor ligand binding core s1s2 g729c mutant]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:08:38 2007''