1f88
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CRYSTAL STRUCTURE OF BOVINE RHODOPSIN
OverviewOverview
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 a, bundle of seven transmembrane alpha helices connected by six loops of, varying lengths. We determined the structure of rhodopsin from diffraction, data extending to 2.8 angstroms resolution. The highly organized structure, in the extracellular region, including a conserved disulfide bridge, forms, a basis for the arrangement of the seven-helix transmembrane motif. The, ground-state chromophore, 11-cis-retinal, holds the transmembrane region, of the protein in the inactive conformation. Interactions of the, chromophore with a cluster of key residues determine the wavelength of the, maximum absorption. Changes in these interactions among rhodopsins, facilitate color discrimination. Identification 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.
About this StructureAbout this Structure
1F88 is a Single protein structure of sequence from [1] with HG, ZN and RET as ligands. The following pages contain interesting information on the relation of 1F88 with [Bacteriorhodopsin], [G Proteins] and [Carotenoid Oxygenase]. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of rhodopsin: A G protein-coupled receptor., Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M, Science. 2000 Aug 4;289(5480):739-45. PMID:10926528
Page seeded by OCA on Sun Nov 18 08:59:53 2007