Editors' ChoiceStructural Biology

Rhodopsin's Structure Revealed

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Science's STKE  08 Aug 2000:
Vol. 2000, Issue 44, pp. tw9
DOI: 10.1126/stke.2000.44.tw9

Heterotrimeric guanine-nucleotide binding proteins (G proteins) that are involved in many different signaling pathways are activated by G protein-coupled receptors (GPCRs), a large family of membrane proteins that respond to a variety of stimuli. Rhodopsins are GPCRs that respond to light and activate the visual transduction pathway. Now Palczewski et al. (see the Perspective by Bourne and Meng) have determined the structure of rhodopsin from diffraction data extending to 2.8 angstroms. The structure reveals the interactions of the ground-state chromophore, 11-cis-retinal, with residues in the seven α-helix transmembrane domain. The chromophore plays a key role in holding the transmembrane region in the inactive conformation. The structure also provides insight into how isomerization of 11-cis-retinal to all-trans-retinal may cause conformational changes that could be transmitted to G proteins at the cytoplasmic surface.

Palczewski, K., Kumasaka, T., Hori, T., Behnke, C.A., Motoshima, H., Fox, B.A., Trong, I.L., Teller, D.C., Okada, T., Stenkamp, R.E., Yamamoto, M., and Miyano, M. (2000) Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289: 739-745. [Abstract] [Full Text]

Bourne, H.R., and Meng, E.C. (2000) Rhodopsin sees the light. Science 289: 733-734. [Full Text]

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