The 'functional' dyad of scorpion toxin Pi1 is not itself a prerequisite for toxin binding to the voltage-gated Kv1.2 potassium channels

Biochemical Journal

Volumn 377, Issue 1, 2004, Pages 25-36

  Mouhat, Stéphanie ^a,b   Mosbah, Amor ^a,b   Visan, Violeta ^c   Wulff, Heike ^d   Delepierre, Muriel ^b   Darbon, Hervé ^e   Grissmer, Stephan ^c   De Waard, Michel ^f   Sabatier, Jean Marc ^a,b  

^a Lab Intl Associe d'Ingenierie B   (France)

^b CNRS   (France)

^c UNIVERSITY OF ULM   (Germany)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e Centre National de la Recherche Scientifique   (France)

^f INSERM   (France)

Author keywords

Functional dyad; K+ channel; Kv1.2 channel; Phosphorylated tyrosine; Pi1; Scorpion toxin

Indexed keywords

AMINO ACIDS; BRAIN; CHEMICAL BONDS; COMPUTER SIMULATION; CROSSLINKING; CYTOLOGY; POTASSIUM; SYNTHESIS (CHEMICAL); TOXIC MATERIALS;

PHOSPHORYLATION;

BIOCHEMISTRY;

SCORPION TOXIN PI1; SCORPION VENOM; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL;

ARTICLE; CONTROLLED STUDY; CROSS LINKING; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; PHOSPHORYLATION; PRIORITY JOURNAL; SCORPION; SIMULATION; SYNAPTOSOME; SYNTHESIS; XENOPUS LAEVIS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELLS, CULTURED; KV1.2 POTASSIUM CHANNEL; LYSINE; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; POTASSIUM CHANNEL BLOCKERS; POTASSIUM CHANNELS; POTASSIUM CHANNELS, VOLTAGE-GATED; PROTEIN STRUCTURE, TERTIARY; RATS; SCORPION VENOMS; SEQUENCE ALIGNMENT; TYROSINE; XENOPUS LAEVIS;

ARACHNIDA; HEXAPODA; SCORPIONES; VERTEBRATA; XENOPUS LAEVIS;

EID: 1642453564     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030115     Document Type: Article

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