NOTICE: Due to a lapse in annual appropriations, most of this website is not being updated. Learn more.
Form submissions will still be accepted but will not receive responses at this time. Sections of this site for programs using non-appropriated funds (such as NVLAP) or those that are excepted from the shutdown (such as CHIPS and NVD) will continue to be updated.
An official website of the United States government
Here’s how you know
Official websites use .gov
A .gov website belongs to an official government organization in the United States.
Secure .gov websites use HTTPS
A lock (
) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.
Rhodopsin is a retinal photoreceptor protein of bipartite structure consisting of the transmembrane protein opsin and the light Sensitive chromophore 11-cis-retinal, linked to opsin via a protonated Schiff base. Studies on rhodopsin have unveiled many structural and functional features that are common to a large and pharmacologically important group of proteins from the G-protein-coupled receptor (GPCR) superfamily, of which rhodopsin is the best-studied member. In this work, the main emphasis will be on structural investigations. In particular, the high-resolution structure of bovine rhodopsin provides a template for understanding how GPCRs work and highlights its central importance to the visual process.
Citation
Annual Review of Biophysics and Biomolecular Structure
Pub Type
Journals
Keywords
crystal structure, G-protein-coupled receptors, phototransduction, rhodopsin, signal transduction, transmembrane protein, vision, vitamin A
Citation
Ridge, K.
(2008),
Rhodopsin Chemistry and Structure, Annual Review of Biophysics and Biomolecular Structure
(Accessed October 10, 2025)