The 9-Arginine residue of α-Conotoxin GI is responsible for its selective high affinity for the αγ agonist site on the electric organ acetylcholine receptor

Biochemistry

Volumn 36, Issue 29, 1997, Pages 9051-9056

  Hann, Richard M ^a   Pagán, Oné R ^a   Gregory, Liza M ^a   Jácome, Tomas ^a   Eterović, Vesna A ^a  

^a SCHOOL OF MEDICINE   (Puerto Rico)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA BUNGAROTOXIN; CHOLINERGIC RECEPTOR; CONOTOXIN; IODINE 125; SYNTHETIC PEPTIDE; TUBOCURARINE CHLORIDE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; ELECTRIC ORGAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; RECEPTOR BINDING;

AMINO ACID SEQUENCE; ANIMALS; ARGININE; BATRACHOTOXINS; BINDING SITES; BINDING, COMPETITIVE; CHOLINERGIC AGONISTS; CONOTOXINS; ELECTRIC ORGAN; MOLECULAR SEQUENCE DATA; MOLLUSK VENOMS; PEPTIDES, CYCLIC; RECEPTORS, CHOLINERGIC; TORPEDO;

EID: 0030791182     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi970807c     Document Type: Article

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