Opsin is present as dimers in COS1 cells: Identification of amino acids at the dimeric interface

Proceedings of the National Academy of Sciences of the United States of America

Volumn 103, Issue 9, 2006, Pages 3054-3059

  Kota, Parvathi ^a   Reeves, Philip J ^a,b   RajBhandary, Uttam L ^a   Khorana, H Gobind ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b UNIVERSITY OF ESSEX   (United Kingdom)

Author keywords

Cross linking; Cysteine mutagenesis; Dimerization; FRET; G protein coupled receptors

Indexed keywords

AMINO ACID; CYAN FLUORESCENT PROTEIN; DIMER; OPSIN; PHENANTHROLINE DERIVATIVE; RHODOPSIN;

AMINO ACID ANALYSIS; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; ATOMIC FORCE MICROSCOPY; CELL STRAIN COS1; CONTROLLED STUDY; CROSS LINKING; DARKNESS; DIMERIZATION; DISULFIDE BOND; ELECTRON MICROSCOPY; FLUORESCENCE RESONANCE ENERGY TRANSFER; GENE FUSION; LIGHT; MOLECULAR INTERACTION; NONHUMAN; PHOTORECEPTOR; PRIORITY JOURNAL; RETINA ROD; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; BINDING SITES; CELL MEMBRANE; CERCOPITHECUS AETHIOPS; COS CELLS; CROSS-LINKING REAGENTS; CYSTEINE; DIMERIZATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; MOLECULAR SEQUENCE DATA; MUTATION; OPSIN; PHENANTHROLINES; PROTEIN STRUCTURE, QUATERNARY;

ANIMALIA;

EID: 33644781659     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0510982103     Document Type: Article

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