Chimeric and point-mutated receptors reveal that a single glycine residue in transmembrane domain 6 is critical for high affinity melatonin binding

Endocrinology

Volumn 141, Issue 3, 2000, Pages 1236-1244

  Gubitz, Amelie K ^b   Reppert, Steven M ^a  

^a MASSACHUSETTS GENERAL HOSPITAL   (United States)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CHIMERIC PROTEIN; GLYCINE; IODINE 125; MELATONIN; MELATONIN RECEPTOR; NUCLEOTIDE; THREONINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CELL STRAIN; CHIMERA; HORMONE RECEPTOR INTERACTION; HUMAN; LIGAND BINDING; NONHUMAN; NUCLEOTIDE SEQUENCE; PINEAL BODY; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; RECEPTOR AFFINITY; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; STEREOCHEMISTRY; STEREOSPECIFICITY; STRUCTURE ACTIVITY RELATION;

EID: 0034464824     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.141.3.7356     Document Type: Article

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