Binding site in eag voltage sensor accommodates a variety of ions and is accessible in closed channel

Biophysical Journal

Volumn 87, Issue 5, 2004, Pages 3110-3121

  Silverman, William R ^a,b   Bannister, John P A ^a   Papazian, Diane M ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATION; MAGNESIUM; MANGANESE; NICKEL; POTASSIUM CHANNEL; ION; METAL; POTASSIUM CHANNEL HERG; RECOMBINANT PROTEIN;

ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CYTOPLASM; ELECTRIC POTENTIAL; EVOKED RESPONSE AUDIOMETRY; GENE MUTATION; HYDROPHOBICITY; PHENOTYPE; SENSOR; AMINO ACID SUBSTITUTION; ANIMAL; CELL CULTURE; CELL MEMBRANE POTENTIAL; CHANNEL GATING; COMPARATIVE STUDY; DOSE RESPONSE; DRUG EFFECT; METABOLISM; OOCYTE; PHYSIOLOGY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; XENOPUS;

AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CELLS, CULTURED; DOSE-RESPONSE RELATIONSHIP, DRUG; ETHER-A-GO-GO POTASSIUM CHANNELS; ION CHANNEL GATING; IONS; MAGNESIUM; MANGANESE; MEMBRANE POTENTIALS; METALS; MUTAGENESIS, SITE-DIRECTED; NICKEL; OOCYTES; POTASSIUM CHANNELS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS;

EID: 16344370100     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.044602     Document Type: Article

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