Inter-residue coupling contributes to high-affinity subtype-selective binding of α-bungarotoxin to nicotinic receptors

Biochemical Journal

Volumn 454, Issue 2, 2013, Pages 311-321

  Sine, Steven M ^a,b   Huang, Sun ^a   Li, Shu Xing ^c   Dacosta, Corrie J B ^a   Chen, Lin ^c,d  

^a MAYO GRADUATE SCHOOL   (United States)

^b Mayo Clinic College of Medicine   (United States)

^c UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^d UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

Crystal structure; Inter residue coupling; Molecular recognition; Neurotoxin; Nicotinic acetylcholine receptor

Indexed keywords

ACETYLCHOLINE; ALPHA BUNGAROTOXIN; IODINE 125; NICOTINIC RECEPTOR; SEROTONIN 3A RECEPTOR; TYROSINE;

ARTICLE; CHIMERA; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISSOCIATION; HUMAN; HUMAN CELL; KINETICS; LIGAND BINDING; MUTATION; PATCH CLAMP; PRIORITY JOURNAL;

AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; BUNGAROTOXINS; BUNGARUS; HEK293 CELLS; HUMANS; LIGANDS; MODELS, MOLECULAR; MUTANT PROTEINS; NEUROTOXINS; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN ISOFORMS; RECEPTORS, NICOTINIC; RECEPTORS, SEROTONIN, 5-HT3; RECOMBINANT FUSION PROTEINS; REPTILIAN PROTEINS; TYROSINE;

EID: 84881519874     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20130638     Document Type: Article

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