2boc

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Revision as of 10:41, 18 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2boc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2boc, resolution 3.01Å" /> '''POTASSIUM CHANNEL K...)
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File:2boc.gif


2boc, resolution 3.01Å

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POTASSIUM CHANNEL KCSA-FAB COMPLEX IN THALLIUM WITH TETRAETHYLARSONIUM (TEAS)

OverviewOverview

Potassium channels catalyze the selective transfer of potassium across the, cell membrane and are essential for setting the resting potential in, cells, controlling heart rate and modulating the firing pattern in, neurons. Tetraethylammonium (TEA) blocks ion conduction through potassium, channels in a voltage-dependent manner from both sides of the membrane., Here we show the structural basis of TEA blockade by cocrystallizing the, prokaryotic potassium channel KcsA with two selective TEA analogs. TEA, binding at both sites alters ion occupancy in the selectivity filter;, these findings underlie the mutual destabilization and voltage-dependence, of TEA blockade. We propose that TEA blocks potassium channels by acting, as a potassium analog at the dehydration transition step during, permeation.

About this StructureAbout this Structure

2BOC is a Protein complex structure of sequences from Mus musculus and Streptomyces lividans with CO, TL and T1A as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of TEA blockade in a model potassium channel., Lenaeus MJ, Vamvouka M, Focia PJ, Gross A, Nat Struct Mol Biol. 2005 May;12(5):454-9. Epub 2005 Apr 24. PMID:15852022

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