Gβγ-activated inwardly rectifying K+ (GIRK) channel activation kinetics via Gαi and Gαo-coupled receptors are determined by Gα-specific interdomain interactions that affect GDP release rates

Journal of Biological Chemistry

Volumn 279, Issue 28, 2004, Pages 29787-29796

  Zhang, Qingli ^a,b   Dickson, Alec ^a   Doupnik, Craig A ^a  

^a UNIVERSITY OF SOUTH FLORIDA   (United States)

^b UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; REACTION KINETICS;

ACTIVATION KINETICS; MUTATIONS;

BIOCHEMISTRY;

AMINO ACID; G PROTEIN COUPLED RECEPTOR; GUANOSINE DIPHOSPHATE; INWARDLY RECTIFYING POTASSIUM CHANNEL; MUSCARINIC M2 RECEPTOR; PERTUSSIS TOXIN; RAS PROTEIN; RECEPTOR SUBUNIT; G PROTEIN COUPLED INWARDLY RECTIFYING POTASSIUM CHANNEL; GUANINE NUCLEOTIDE BINDING PROTEIN BETA SUBUNIT; HYBRID PROTEIN; INHIBITORY GUANINE NUCLEOTIDE BINDING PROTEIN; ISOPROTEIN; POTASSIUM CHANNEL;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CHANNEL GATING; CHIMERA; DELETION MUTANT; INWARDLY RECTIFYING POTASSIUM CHANNEL KIR3.1; INWARDLY RECTIFYING POTASSIUM CHANNEL KIR3.2A; KINETICS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; REGULATORY MECHANISM; XENOPUS; AMINO ACID SEQUENCE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECT; GENETICS; METABOLISM; MOLECULAR GENETICS; OOCYTE; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; XENOPUS LAEVIS;

ANIMALIA;

AMINO ACID SEQUENCE; ANIMALS; G PROTEIN-COUPLED INWARDLY-RECTIFYING POTASSIUM CHANNELS; GTP-BINDING PROTEIN ALPHA SUBUNITS, GI-GO; GTP-BINDING PROTEIN BETA SUBUNITS; GUANOSINE DIPHOSPHATE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OOCYTES; PERTUSSIS TOXIN; POTASSIUM CHANNELS; POTASSIUM CHANNELS, INWARDLY RECTIFYING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, G-PROTEIN-COUPLED; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; XENOPUS LAEVIS;

EID: 3142723472     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M403359200     Document Type: Article

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