3atd: Difference between revisions
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==Crystal Structure of the Kir3.2 Cytoplasmic Domain (Na+-free crystal soaked in 10 mM Gadolinium chloride and 10 mM magnesium chloride)== | ==Crystal Structure of the Kir3.2 Cytoplasmic Domain (Na+-free crystal soaked in 10 mM Gadolinium chloride and 10 mM magnesium chloride)== | ||
<StructureSection load='3atd' size='340' side='right' caption='[[3atd]], [[Resolution|resolution]] 3.01Å' scene=''> | <StructureSection load='3atd' size='340' side='right' caption='[[3atd]], [[Resolution|resolution]] 3.01Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3atd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3atd]] is a 1 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=3ATD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ATD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GD:GADOLINIUM+ATOM'>GD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GD:GADOLINIUM+ATOM'>GD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3agw|3agw]], [[2e4f|2e4f]], [[3at8|3at8]], [[3at9|3at9]], [[3ata|3ata]], [[3atb|3atb]], [[3ate|3ate]], [[3atf|3atf]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3agw|3agw]], [[2e4f|2e4f]], [[3at8|3at8]], [[3at9|3at9]], [[3ata|3ata]], [[3atb|3atb]], [[3ate|3ate]], [[3atf|3atf]]</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=3atd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3atd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3atd RCSB], [http://www.ebi.ac.uk/pdbsum/3atd 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=3atd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3atd OCA], [http://pdbe.org/3atd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3atd RCSB], [http://www.ebi.ac.uk/pdbsum/3atd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3atd 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 3atd" 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 00:31, 6 August 2016
Crystal Structure of the Kir3.2 Cytoplasmic Domain (Na+-free crystal soaked in 10 mM Gadolinium chloride and 10 mM magnesium chloride)Crystal Structure of the Kir3.2 Cytoplasmic Domain (Na+-free crystal soaked in 10 mM Gadolinium chloride and 10 mM magnesium chloride)
Structural highlights
Publication Abstract from PubMedIon channels gate at membrane-embedded domains by changing their conformation along the ion conduction pathway. Inward rectifier K(+) (Kir) channels possess a unique extramembrane cytoplasmic domain that extends this pathway. However, the relevance and contribution of this domain to ion permeation remain unclear. By qualitative x-ray crystallographic analysis, we found that the pore in the cytoplasmic domain of Kir3.2 binds cations in a valency-dependent manner and does not allow the displacement of Mg(2+) by monovalent cations or spermine. Electrophysiological analyses revealed that the cytoplasmic pore of Kir3.2 selectively binds positively charged molecules and has a higher affinity for Mg(2+) when it has a low probability of being open. The selective blocking of chemical modification of the side chain of pore-facing residues by Mg(2+) indicates that the mode of binding of Mg(2+) is likely to be similar to that observed in the crystal structure. These results indicate that the Kir3.2 crystal structure has a closed conformation with a negative electrostatic field potential at the cytoplasmic pore, the potential of which may be controlled by conformational changes in the cytoplasmic domain to regulate ion diffusion along the pore. Interactions of cations with the cytoplasmic pores of inward rectifier K(+) channels in the closed state.,Inanobe A, Nakagawa A, Kurachi Y J Biol Chem. 2011 Dec 2;286(48):41801-11. Epub 2011 Oct 9. PMID:21982822[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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