3t1c: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal Structure of NaK Channel D66Y Mutant== | ==Crystal Structure of NaK Channel D66Y Mutant== | ||
<StructureSection load='3t1c' size='340' side='right' caption='[[3t1c]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='3t1c' size='340' side='right' caption='[[3t1c]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3t1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3t1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baccr Baccr]. 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> | </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='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= | <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=226900 BACCR])</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> | <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://pdbe.org/3t1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t1c RCSB], [http://www.ebi.ac.uk/pdbsum/3t1c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t1c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 16: | Line 17: | ||
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 3t1c" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 23: | Line 25: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Baccr]] | ||
[[Category: Jiang, Y]] | [[Category: Jiang, Y]] | ||
[[Category: Raghunathan, S]] | [[Category: Raghunathan, S]] | ||
Revision as of 14:31, 10 December 2016
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
|
| ||||||||||||||||||||