3atd: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3atd]] 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=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> | |||
<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> | |||
</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]] | ||