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==Cytoplasmic domain of inward rectifier potassium channel Kir3.2 in complex with cadmium== | ==Cytoplasmic domain of inward rectifier potassium channel Kir3.2 in complex with cadmium== | ||
<StructureSection load='3auw' size='340' side='right' caption='[[3auw]], [[Resolution|resolution]] 3.56Å' scene=''> | <StructureSection load='3auw' size='340' side='right' caption='[[3auw]], [[Resolution|resolution]] 3.56Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3auw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3auw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AUW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AUW FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3agw|3agw]], [[2e4f|2e4f]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3agw|3agw]], [[2e4f|2e4f]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Kcnj6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Kcnj6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3auw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3auw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3auw RCSB], [http://www.ebi.ac.uk/pdbsum/3auw PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3auw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3auw OCA], [http://pdbe.org/3auw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3auw RCSB], [http://www.ebi.ac.uk/pdbsum/3auw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3auw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3auw" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Lk3 transgenic mice]] | ||
[[Category: Inanobe, A]] | [[Category: Inanobe, A]] | ||
[[Category: Kurachi, Y]] | [[Category: Kurachi, Y]] | ||
Revision as of 22:57, 5 August 2016
Cytoplasmic domain of inward rectifier potassium channel Kir3.2 in complex with cadmiumCytoplasmic domain of inward rectifier potassium channel Kir3.2 in complex with cadmium
Structural highlights
Publication Abstract from PubMedThe gate at the pore-forming domain of potassium channels is allosterically controlled by a stimulus-sensing domain. Using Cd(2)(+) as a probe, we examined the structural elements responsible for gating in an inward-rectifier K(+) channel (Kir3.2). One of four endogenous cysteines facing the cytoplasm contributes to a high-affinity site for inhibition by internal Cd(2)(+). Crystal structure of its cytoplasmic domain in complex with Cd(2)(+) reveals that octahedral coordination geometry supports the high-affinity binding. This mode of action causes the tethering of the N-terminus to CD loop in the stimulus-sensing domain, suggesting that their conformational changes participate in gating and Cd(2)(+) inhibits Kir3.2 by trapping the conformation in the closed state like "inverse agonist". Inverse agonist-like action of cadmium on G-protein-gated inward-rectifier K(+) channels.,Inanobe A, Matsuura T, Nakagawa A, Kurachi Y Biochem Biophys Res Commun. 2011 Apr 8;407(2):366-71. Epub 2011 Mar 17. PMID:21396912[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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