3t1c: Difference between revisions
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[[ | ==Crystal Structure of NaK Channel D66Y Mutant== | ||
<StructureSection load='3t1c' size='340' side='right' caption='[[3t1c]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3t1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T1C FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ouf|3ouf]], [[3t2m|3t2m]], [[3t4d|3t4d]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BC_0669 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus])</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=3t1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t1c RCSB], [http://www.ebi.ac.uk/pdbsum/3t1c PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structural and functional conversion of the nonselective NaK channel to a K(+) selective channel (NaK2K) allows us to identify two key residues, Tyr and Asp in the filter sequence of TVGYGD, that participate in interactions central to stabilizing the K(+) channel selectivity filter. By using protein crystallography and channel electrophysiology, we demonstrate that the K(+) channel filter exists as an energetically strained structure and requires these key protein interactions working in concert to hold the filter in the precisely defined four-sited configuration that is essential for selective K(+) permeation. Disruption of either interaction, as tested on both the NaK2K and eukaryotic K(v)1.6 channels, can reduce or completely abolish K(+) selectivity and in some cases may also lead to channel inactivation due to conformational changes at the filter. Additionally, on the scaffold of NaK we recapitulate the protein interactions found in the filter of the Kir channel family, which uses a distinct interaction network to achieve similar stabilization of the filter. | |||
Protein interactions central to stabilizing the K+ channel selectivity filter in a four-sited configuration for selective K+ permeation.,Sauer DB, Zeng W, Raghunathan S, Jiang Y Proc Natl Acad Sci U S A. 2011 Sep 20. PMID:21933962<ref>PMID:21933962</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Potassium Channel|Potassium Channel]] | *[[Potassium Channel|Potassium Channel]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Bacillus cereus]] | [[Category: Bacillus cereus]] | ||
[[Category: Jiang, Y | [[Category: Jiang, Y]] | ||
[[Category: Raghunathan, S | [[Category: Raghunathan, S]] | ||
[[Category: Sauer, D B | [[Category: Sauer, D B]] | ||
[[Category: Zeng, W | [[Category: Zeng, W]] | ||
[[Category: Ion channel]] | [[Category: Ion channel]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
Revision as of 16:04, 9 December 2014
Crystal Structure of NaK Channel D66Y MutantCrystal Structure of NaK Channel D66Y Mutant
Structural highlights
Publication Abstract from PubMedThe structural and functional conversion of the nonselective NaK channel to a K(+) selective channel (NaK2K) allows us to identify two key residues, Tyr and Asp in the filter sequence of TVGYGD, that participate in interactions central to stabilizing the K(+) channel selectivity filter. By using protein crystallography and channel electrophysiology, we demonstrate that the K(+) channel filter exists as an energetically strained structure and requires these key protein interactions working in concert to hold the filter in the precisely defined four-sited configuration that is essential for selective K(+) permeation. Disruption of either interaction, as tested on both the NaK2K and eukaryotic K(v)1.6 channels, can reduce or completely abolish K(+) selectivity and in some cases may also lead to channel inactivation due to conformational changes at the filter. Additionally, on the scaffold of NaK we recapitulate the protein interactions found in the filter of the Kir channel family, which uses a distinct interaction network to achieve similar stabilization of the filter. Protein interactions central to stabilizing the K+ channel selectivity filter in a four-sited configuration for selective K+ permeation.,Sauer DB, Zeng W, Raghunathan S, Jiang Y Proc Natl Acad Sci U S A. 2011 Sep 20. PMID:21933962[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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