Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin

Science

Volumn 274, Issue 5288, 1996, Pages 768-770

  Farrens, David L ^a,c   Altenbach, Christian ^b   Yang, Ke ^a,d   Hubbell, Wayne L ^b   Khorana, H Gobind ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b JULES STEIN EYE INSTITUTE   (United States)

^c OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^d MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GUANINE NUCLEOTIDE BINDING PROTEIN; RHODOPSIN; TRANSDUCIN;

ARTICLE; CONFORMATIONAL TRANSITION; CROSS LINKING; ISOMERISM; PHOTOACTIVATION; PRIORITY JOURNAL; PROTEIN STRUCTURE; SPIN LABELING;

AMINO ACID SEQUENCE; CYSTEINE; DISULFIDES; ELECTRON SPIN RESONANCE SPECTROSCOPY; EYE PROTEINS; LIGHT; MOLECULAR SEQUENCE DATA; MUTATION; OXIDATION-REDUCTION; PHENANTHROLINES; PROTEIN KINASES; PROTEIN STRUCTURE, SECONDARY; RHODOPSIN; RHODOPSIN KINASE; SERINE ENDOPEPTIDASES; SPIN LABELS; TRANSDUCIN;

EID: 0029907599     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.274.5288.768     Document Type: Article

References (41)

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40. In thodopsin, a series of nistidine obstructions at the cytopiasmic ends of helices C and G, created high-affinity metal-ion binding saas. Activation of trenducine was biocked when metal was bound to the high-afinity stss, prsurably because of effective cross-linking of hollces O and F, consistant with reads orsented here (S, Sheikh, T. Zvyaga. O. Zyyaga, O. Lichterge, T. Sakinar, H. Boume, Nature, in press).
41. 139 mutant gene. Supported by NIH grants EY05216 (W.L.H.) and GM28289 (H.G.K.), NIH National Research Service Award EY06465 (D.L.F.), and the Jules Stein Professorship endowment (W.L.H.).