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Primary structure of C-terminal functional sites in ovine rhodopsin

Nature volume 293, pages 314–316 (1981)Cite this article

Abstract

Rhodopsin is the primary photoreceptor protein in the vertebrate retina. The functional complex consists of the polypeptide, opsin, to which is bound a molecule of 11-cis-retinal. An absorbed photon of light induces electronic changes in this chromophore, resulting in its isomerization to the all-trans form1 and the triggering of a series of spectrally-defined con-formational changes in the protein. This ‘activation’ of rhodopsin promotes biochemical events which result in the transmission of an integrated response to the brain (for reviews, see refs 2–4). Here we report the amino acid sequence of the C-terminal third of the ovine protein, in which we identify the retinal-binding and phosphorylation sites.

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Authors and Affiliations

  1. Department of Biochemistry, University of Leeds, 9 Hyde Terrace, Leeds, LS2 9LS, UK

    John B. C. Findlay, Michael Brett & Darryl J. C. Pappin

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  1. John B. C. Findlay
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  2. Michael Brett
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  3. Darryl J. C. Pappin
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Findlay, J., Brett, M. & Pappin, D. Primary structure of C-terminal functional sites in ovine rhodopsin. Nature 293, 314–316 (1981). https://doi.org/10.1038/293314a0

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