Critical molecular determinants of voltage-gated sodium channel sensitivity to μ-conotoxins GIIIA/B

Molecular Pharmacology

Volumn 61, Issue 5, 2002, Pages 1192-1201

  Cummins, Theodore R ^a   Aglieco, Fabio ^a   Dib Hajj, Sulayman D ^a  

^a PVA/EPVA Neurosci Research Center   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; CD36 ANTIGEN; CONOTOXIN; GLYCOPROTEIN IIIA; LEUCINE; LYSINE; MU CONOTOXIN; SERINE; SODIUM CHANNEL; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CHANNEL GATING; ELECTROPHYSIOLOGY; HUMAN; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN INTERACTION; RAT; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ANIMALS; CELLS, CULTURED; CONOTOXINS; HUMANS; MOLECULAR SEQUENCE DATA; PATCH-CLAMP TECHNIQUES; POINT MUTATION; PROTEIN STRUCTURE, TERTIARY; RATS; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM CHANNELS;

EID: 0036237688     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.61.5.1192     Document Type: Article

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4. Extrapore residues of the S5-S6 loop of domain 2 of the voltage-gated skeletal muscle sodium channel (rSkM1) contribute to the μ-conotoxin GIIIA binding site
5. Extrapore residues of the S5-S6 loop of domain 2 of the voltage-gated skeletal muscle sodium channel (rSkM1) contribute to the μ-conotoxin GIIIA binding site
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