2ih3: Difference between revisions
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'''Ion selectivity in a semi-synthetic K+ channel locked in the conductive conformation''' | '''Ion selectivity in a semi-synthetic K+ channel locked in the conductive conformation''' | ||
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[[Category: Muir, T W.]] | [[Category: Muir, T W.]] | ||
[[Category: Valiyaveetil, F I.]] | [[Category: Valiyaveetil, F I.]] | ||
[[Category: | [[Category: Ion channel d-amino acid semi-synthetic]] | ||
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Revision as of 07:29, 4 May 2008
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. 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 Page seeded by OCA on Sun May 4 07:29:45 2008