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Rhodopsin is a member of the G-protein coupled receptor (GPCR) family. Rhodopsin is the

common GPCR structure used to understand functionality of G-protein coupled receptors. Rhodopsin is commonly found in the photoreceptors in the retina, specifically in the rod photoreceptors and become activated by photons of light. Rhodopsin contains a chromophore (compound that absorbs light), specifically 11-cis-retinal, which when active recruites G proteins to transmit a signaling cascade in neural impulses to the gray matter of the occipital lobe. Once the receptor has been activated, a new rhodopsin needs to be regenerated. Rhodopsin is located in the rod outer segment (ROS) which consists of stacked disks enclosed by a membrane. The entire family of GPCR’s have the common structure of seven alpha-helices across membranes. Rhodopsin’s structure changes upon photoactivation. The sixth helix bends away from the seventh creating a pocket that allows for binding of a G protein. A salt bridge covers this pocket until the helices shift away from one another. Once the G protein has bound then the signal can be transmitted to the occipital lobe. Over 120 point mutations to rhodopsin have been identified which can lead to night blindness and more several visual problems^[1].

Function

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Disease

Relevance

Stuff and things

We are here

Dirty pickles

Monkeys

Monday

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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References

Zhou, X Edward, Karsten Melcher, and H Eric Xu. “Structure and Activation of Rhodopsin.” Acta Pharmacologica Sinica 33.3 (2012): 291–299. PMC . Web. 11 Feb. 2018. Palczewski, Krzysztof. “G Protein–Coupled Receptor Rhodopsin.” Annual review of biochemistry 75 (2006): 743–767. PMC . Web. 11 Feb. 2018.

1. ↑ Sakmar TP. Structure of rhodopsin and the superfamily of seven-helical receptors: the same and not the same. Curr Opin Cell Biol. 2002 Apr;14(2):189-95. PMID:11891118