A mutation in S6 of Shaker potassium channels decreases the K+ affinity of an ion binding site revealing ion-ion interactions in the pore

Journal of General Physiology

Volumn 112, Issue 2, 1998, Pages 243-257

  Ogielska, Eva M ^a   Aldrich, Richard W ^a  

^a STANFORD UNIVERSITY   (United States)

Author keywords

Ion selectivity; K+ affinity; Na+ permeation; S6; Shaker

Indexed keywords

BARIUM; MEGLUMINE; POTASSIUM CHANNEL; POTASSIUM CHLORIDE; POTASSIUM ION; SODIUM CHLORIDE; SODIUM ION; TETRYLAMMONIUM;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; MUTATION; NONHUMAN; OOCYTE; POTASSIUM CURRENT; SODIUM CURRENT; XENOPUS LAEVIS;

AMINO ACID SEQUENCE; ANIMALS; BARIUM; BINDING SITES; BIOLOGICAL TRANSPORT; ION CHANNEL GATING; MOLECULAR SEQUENCE DATA; MUTAGENESIS; OOCYTES; PATCH-CLAMP TECHNIQUES; POTASSIUM; POTASSIUM CHANNELS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SHAKER SUPERFAMILY OF POTASSIUM CHANNELS; SODIUM; XENOPUS LAEVIS;

EID: 0031822014     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.112.2.243     Document Type: Article

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