Single-cysteine substitution mutants at amino acid positions 306-321 in rhodopsin, the sequence between the cytoplasmic end of helix VII and the palmitoylation sites: Sulfhydryl reactivity and transducin activation reveal a tertiary structure

Biochemistry

Volumn 38, Issue 25, 1999, Pages 7925-7930

  Cai, Kewen ^a   Klein Seetharaman, Judith ^a   Farrens, David ^a,c   Zhang, Cheng ^a,d   Altenbach, Christian ^b   Hubbell, Wayne L ^b   Gobind Khorana, H ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b JULES STEIN EYE INSTITUTE   (United States)

^c OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^d MILLENNIUM PHARMACEUTICALS INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

11 CIS RETINAL; OPSIN; RHODOPSIN; TRANSDUCIN;

AMINO ACID SUBSTITUTION; ARTICLE; CHROMATOPHORE; PALMITOYLATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CATTLE; COS CELLS; CYSTEINE; CYTOPLASM; DISULFIDES; LEUCINE; LIGHT; MOLECULAR SEQUENCE DATA; PALMITIC ACID; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PYRIDINES; RHODOPSIN; SPECTROMETRY, FLUORESCENCE; SULFHYDRYL REAGENTS; TRANSDUCIN; TYROSINE;

EID: 0033594866     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9900119     Document Type: Article

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