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Crystal structure of rhodopsin: a G protein-coupled receptor (2000)
| Venue: | LeTrong I, Teller DC, Okada T, Stenkamp RE et |
| Citations: | 376 - 4 self |
BibTeX
@ARTICLE{Palczewski00crystalstructure,
author = {Krzysztof Palczewski and Takashi Kumasaka and Tetsuya Hori and Craig A. Behnke and Hiroyuki Motoshima and Brian A. Fox and Isolde Le Trong and David C. Teller and Tetsuji Okada and Ronald E. Stenkamp and Masaki Yamamoto and Masashi Miyano},
title = {Crystal structure of rhodopsin: a G protein-coupled receptor},
journal = {LeTrong I, Teller DC, Okada T, Stenkamp RE et},
year = {2000},
pages = {739--745}
}
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Abstract
Heterotrimeric guanine nucleotideÐbinding protein (G protein)Ðcoupled recep-tors (GPCRs) respond to a variety of different external stimuli and activate G proteins. GPCRs share many structural features, including a bundle of seven transmembrane a helices connected by six loops of varying lengths. We de-termined the structure of rhodopsin from diffraction data extending to 2.8 angstroms resolution. The highly organized structure in the extracellular region, including a conserved disulÞde bridge, forms a basis for the arrangement of the seven-helix transmembrane motif. The ground-state chromophore, 11-cis-ret-inal, holds the transmembrane region of the protein in the inactive confor-mation. Interactions of the chromophore with a cluster of key residues deter-mine the wavelength of the maximum absorption. Changes in these interactions among rhodopsins facilitate color discrimination. IdentiÞcation of a set of residues that mediate interactions between the transmembrane helices and the cytoplasmic surface, where G-protein activation occurs, also suggests a possible structural change upon photoactivation.
