Stable cation coordination at a single outer pore residue defines permeation properties in Kir channels

FEBS Letters

Volumn 466, Issue 1, 2000, Pages 115-120

  Wischmeyer, Erhard ^a   Döring, Frank ^a   Karschin, Andreas ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

Anomalous mole fraction; Inwardly rectifying K channel; Ion selectivity; Kir2.1; Kir7.1; Multi ion pore

Indexed keywords

POTASSIUM CHANNEL;

ANIMAL CELL; ARTICLE; BINDING SITE; CELL MEMBRANE PERMEABILITY; CELL MEMBRANE POTENTIAL; CHANNEL GATING; ION CONDUCTANCE; ION CURRENT; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN EXPRESSION; XENOPUS;

ANIMALS; BINDING SITES; FEMALE; HUMANS; MEMBRANE POTENTIALS; MUTAGENESIS, SITE-DIRECTED; OOCYTES; PERMEABILITY; POTASSIUM; POTASSIUM CHANNELS; POTASSIUM CHANNELS, INWARDLY RECTIFYING; RATS; RECOMBINANT PROTEINS; XENOPUS LAEVIS;

EID: 0342545978     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(99)01769-X     Document Type: Article

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