Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor

• DOI: 10.1126/science.289.5480.739
• Publication Date: 2002-07-27T09:35:18Z
• Authors: Krzysztof Palczewski; Takashi Kumasaka; Tetsuya Hori; Craig A. Behnke; Hiroyuki Motoshima; Brian A. Fox; Isolde Le Trong; David C. Teller; Tetsuji Okada; Ronald E. Stenkamp; Masaki Yamamoto; Masashi Miyano
• Keywords: Structural motif; Transducin

Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) respond to a variety of different external stimuli and activate G proteins. GPCRs share many structural features, including bundle seven transmembrane alpha helices connected by six loops varying lengths. We determined the structure rhodopsin from diffraction data extending 2.8 angstroms resolution. The highly organized in extracellular region, conserved disulfide bridge, forms basis for arrangement seven-helix motif. ground-state chromophore, 11-cis-retinal, holds region inactive conformation. Interactions chromophore with cluster key residues determine wavelength maximum absorption. Changes these interactions among rhodopsins facilitate color discrimination. Identification set that mediate between cytoplasmic surface, where G-protein activation occurs, also suggests possible change upon photoactivation.