S3b amino acid substitutions and ancillary subunits alter the affinity of Heteropoda venatoria toxin 2 for Kv4.3

Molecular Pharmacology

Volumn 76, Issue 1, 2009, Pages 125-133

  DeSimone, Christopher V ^a   Lu, YiChun ^a   Bondarenko, Vladimir E ^b   Morales, Michael J ^a  

^a UNIVERSITY AT BUFFALO   (United States)

^b GEORGIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYSTINE; HANATOXIN; RECOMBINANT HETEROPODA VENATORIA TOXIN 2; SHAL POTASSIUM CHANNEL; SPIDER VENOM; TOXIN; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL KV4.3;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; DRUG BINDING; FEMALE; HETEROPODA VENATORIA; HYDROPHOBICITY; MOLECULAR INTERACTION; MUTANT; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SPIDER;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; DOSE-RESPONSE RELATIONSHIP, DRUG; FEMALE; MOLECULAR SEQUENCE DATA; PROTEIN SUBUNITS; SHAB POTASSIUM CHANNELS; SHAL POTASSIUM CHANNELS; SPIDER VENOMS; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS; XENOPUS LAEVIS;

EID: 67649834430     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.109.055657     Document Type: Article

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