2ih1 | pdb_00002ih1

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

spinqualitylabelsall models 2ih1, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ih1 is a 3 chain structure with sequence from Mus musculus and Streptomyces lividans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1EM, K NonStd Res: DAL Related: 2ih3 Gene: kcsA, skc1 (Streptomyces lividans) Resources: FirstGlance, OCA, RCSB, PDBsum 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 PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monoclonal Antibody Potassium Channel

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