Primary structure of C-terminal functional sites in ovine rhodopsin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1981-09

AUTHORS

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

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. More... »

PAGES

314-316

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/293314a0

DOI

http://dx.doi.org/10.1038/293314a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1017208813

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7278988


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