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Article

Partial agonist activity of 11-cis-retinal in rhodopsin mutants.

The Journal of biological chemistry - 12 Sept 1997

Han M, Lou J, Nakanishi K, Sakmar T P, Smith S O

Abstract excerpt

Rhodopsin, the photoreceptor molecule of the vertebrate rod cell, is a G protein-coupled receptor. Rhodopsin consists of the opsin apoprotein and its 11-cis-retinal chromophore, which is covalently bound to a specific lysine residue by a stable protonated Schiff base linkage. Rhodopsin activation occurs when light causes photoisomerization of the 11-cis chromophore to its all-trans form. The all-trans chromophore...

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PMID: 9287308
DOI: 10.1074/jbc.272.37.23081

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Partial agonist activity of 11-cis-retinal in rhodopsin mutants.PMID 9287308Read ↗

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Engineering a "steric doorstop" in rhodopsin: converting an inverse agonist to an agonist.Semantic proximity Read ↗

Effect of channel mutations on the uptake and release of the retinal ligand in opsin.Semantic proximity Read ↗

6-s-cis Conformation and polar binding pocket of the retinal chromophore in the photoactivated state of rhodopsin.Semantic proximity Read ↗

Light-stable rhodopsin. II. An opsin mutant (TRP-265----Phe) and a retinal analog with a nonisomerizable 11-cis configuration form a photostable chromophore.Semantic proximity Read ↗

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