1dsx: Difference between revisions
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==KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT== | ==KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT== | ||
<StructureSection load='1dsx' size='340' side='right' caption='[[1dsx]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1dsx' size='340' side='right' caption='[[1dsx]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dsx]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DSX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DSX FirstGlance]. <br> | <table><tr><td colspan='2'>[[1dsx]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DSX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DSX FirstGlance]. <br> | ||
</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=1dsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dsx OCA], [http://pdbe.org/1dsx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dsx RCSB], [http://www.ebi.ac.uk/pdbsum/1dsx PDBsum]</span></td></tr> | </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=1dsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dsx OCA], [http://pdbe.org/1dsx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dsx RCSB], [http://www.ebi.ac.uk/pdbsum/1dsx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dsx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/1dsx_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/1dsx_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1dsx" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1dsx" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:59, 13 December 2017
KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANTKV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT
Structural highlights
Function[KCNA2_RAT] Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedKv voltage-gated potassium channels share a cytoplasmic assembly domain, T1. Recent mutagenesis of two T1 C-terminal loop residues implicates T1 in channel gating. However, structural alterations of these mutants leave open the question concerning direct involvement of T1 in gating. We find in mammalian Kv1.2 that gating depends critically on residues at complementary T1 surfaces in an unusually polar interface. An isosteric mutation in this interface causes surprisingly little structural alteration while stabilizing the closed channel and increasing the stability of T1 tetramers. Replacing T1 with a tetrameric coiled-coil destabilizes the closed channel. Together, these data suggest that structural changes involving the buried polar T1 surfaces play a key role in the conformational changes leading to channel opening. The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel.,Minor DL, Lin YF, Mobley BC, Avelar A, Jan YN, Jan LY, Berger JM Cell. 2000 Sep 1;102(5):657-70. PMID:11007484[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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