2ih3

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Revision as of 13:11, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="2ih3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ih3, resolution 1.72Å" /> '''Ion selectivity in a...)
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File:2ih3.gif


2ih3, resolution 1.72Å

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Ion selectivity in a semi-synthetic K+ channel locked in the conductive conformation

OverviewOverview

Potassium channels are K+-selective protein pores in cell membrane. The, selectivity filter is the functional unit that allows K+ channels to, distinguish potassium (K+) and sodium (Na+) ions. The filter's structure, depends on whether K+ or Na+ ions are bound inside it. We synthesized a K+, channel containing the d-enantiomer of alanine in place of a conserved, glycine and found by x-ray crystallography that its filter maintains the, K+ (conductive) structure in the presence of Na+ and very low, concentrations of K+. This channel conducts Na+ in the absence of K+ but, not in the presence of K+. These findings demonstrate that the ability of, the channel to adapt its structure differently to K+ and Na+ is a, fundamental aspect of ion selectivity, as is the ability of multiple K+, ions to compete effectively with Na+ for the conductive filter.

About this StructureAbout this Structure

2IH3 is a Single protein structure of sequence from Mus musculus and Streptomyces lividans with K and 1EM as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Ion selectivity in a semisynthetic K+ channel locked in the conductive conformation., Valiyaveetil FI, Leonetti M, Muir TW, Mackinnon R, Science. 2006 Nov 10;314(5801):1004-7. PMID:17095703

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