A single β subunit M2 domain residue controls the picrotoxin sensitivity of αβ heteromeric glycine receptor chloride channels

Journal of Neurochemistry

Volumn 76, Issue 4, 2001, Pages 1109-1120

  Shan, Qiang ^a   Haddrill, Justine L ^a   Lynch, Joseph W ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

Allosteric inhibition; Ligand gated ion channel; Substituted cysteine accessibility method; Threonine ring

Indexed keywords

CHLORIDE CHANNEL; CYSTEINE; GLYCINE RECEPTOR; PICROTOXIN; RECEPTOR SUBUNIT; THREONINE;

ALLOSTERISM; ARTICLE; BETA CHAIN; COMPETITIVE INHIBITION; GENE MUTATION; HUMAN; HUMAN CELL; INHIBITION KINETICS; PRIORITY JOURNAL; PROTEIN DOMAIN; RECEPTOR AFFINITY;

ALLOSTERIC REGULATION; AMINO ACID SUBSTITUTION; BINDING SITES; BINDING, COMPETITIVE; CELL LINE; CHLORIDE CHANNELS; DOSE-RESPONSE RELATIONSHIP, DRUG; GLYCINE; HUMANS; KIDNEY; MESYLATES; MUTAGENESIS, SITE-DIRECTED; PICROTOXIN; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; RECEPTORS, GLYCINE; SEQUENCE HOMOLOGY, AMINO ACID; SULFHYDRYL REAGENTS;

EID: 0035112674     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2001.00124.x     Document Type: Article

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