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3atb
From Proteopedia
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| - | + | ==Crystal Structure of the Kir3.2 Cytoplasmic Domain (Na+-free crystal soaked in 10 mM Gadolinium chloride)== | |
| - | + | <StructureSection load='3atb' size='340' side='right' caption='[[3atb]], [[Resolution|resolution]] 3.51Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3atb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ATB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ATB 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> | ||
| + | <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]], [[3atd|3atd]], [[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=3atb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3atb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3atb RCSB], [http://www.ebi.ac.uk/pdbsum/3atb PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ion 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<ref>PMID:21982822</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | |||
| + | ==See Also== | ||
| + | *[[Potassium Channel|Potassium Channel]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Inanobe, A | + | [[Category: Inanobe, A]] |
| - | [[Category: Kurachi, Y | + | [[Category: Kurachi, Y]] |
[[Category: Beta-barrel]] | [[Category: Beta-barrel]] | ||
[[Category: Cytoplasmic assembly]] | [[Category: Cytoplasmic assembly]] | ||
Revision as of 14:00, 18 December 2014
Crystal Structure of the Kir3.2 Cytoplasmic Domain (Na+-free crystal soaked in 10 mM Gadolinium chloride)
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