Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state.
نویسندگان
چکیده
منابع مشابه
Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187.
Cysteine residues 110 and 187 are essential for the formation of the correct bovine rhodopsin structure (Karnik, S. S., Sakmar, T. P., Chen, H.-B., and Khorana, H. G. (1988) Proc. Natl. Acad. Sci. U. S. A. 85, 8459-8463). We now show that the sulfhydryl groups of these 2 cysteine residues interact to form a disulfide bond. Rhodopsin mutants containing cysteine----serine substitutions were prepa...
متن کاملCysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin.
To investigate the role of different cysteine residues in bovine rhodopsin, a series of mutants were prepared in which the cysteine residues were systematically replaced by serines. The mutant genes were expressed in monkey kidney cells (COS-1) and the mutant opsins were evaluated for their levels of expression, glycosylation patterns, and ability to form the chromophore characteristic of rhodo...
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15 صفحه اولStructure and function in rhodopsin: the fate of opsin formed upon the decay of light-activated metarhodopsin II in vitro.
We report that the light-activated bovine metarhodopsin II, upon decay, first forms opsin in the correctly folded form. The latter binds 11-cis-retinal and regenerates the native rhodopsin chromophore. However, when the opsin formed upon metarhodopsin II decay is kept in 0.1% dodecyl maltoside, it converts in a time-dependent manner to a form(s) that does not bind 11-cis-retinal. On subsequent ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1994
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.91.9.4029