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Projection structure of rhodopsin

Nature volume 362, pages 770772 (22 April 1993) | Download Citation

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Abstract

LIGHT absorption by the visual pigment rhodopsin1,2 triggers, through G-protein coupling, a cascade of events in the outer segment of the rod cell of the vertebrate retina that results in membrane hyperpolarization and nerve excitation3–5. Rhodopsin, which contains 348 amino acids6–8, has seven helices that cross the disk membrane6,9 and its amino terminus is extracellular. A wealth of biochemical data is available for rhodopsin: 11-cis retinal is bound10 to lysine 296 in helix VII; glutamic acid 113 on helix III is the counterion to the protonated Schiff's base11,12; a disulphide bridge, cystine 110–187, connects helix III to the second extracellular loop e2 (refs 13, 14); the carboxy terminus has two palmitoylated cysteines forming a cytoplasmic loop i4 (ref. 15); three intracellular loops i2, i3 and i4 mediate activation of the heterotrimeric G protein transducin16,17; glutamic acid 135 and arginine 136 at the cytoplasmic end of helix III affect binding of transducin18. But to provide a framework to interpret these data, not only for rhodopsin but for other G-protein-coupIed receptors, requires the structure to be determined. Here we present a projection map of rhodopsin showing the configuration of the helices.

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  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK

    • Gebhard F. X. Schertler
    • , Claudio Villa
    •  & Richard Henderson

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https://doi.org/10.1038/362770a0

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