1F88
CRYSTAL STRUCTURE OF BOVINE RHODOPSIN
Summary for 1F88
| Entry DOI | 10.2210/pdb1f88/pdb |
| Descriptor | RHODOPSIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | photoreceptor, g protein-coupled receptor, membrane protein, retinal protein, visual pigment, signaling protein |
| Biological source | Bos taurus (cattle) |
| Cellular location | Membrane; Multi-pass membrane protein: P02699 |
| Total number of polymer chains | 2 |
| Total formula weight | 81956.71 |
| Authors | Okada, T.,Palczewski, K.,Stenkamp, R.E.,Miyano, M. (deposition date: 2000-06-29, release date: 2000-08-04, Last modification date: 2024-10-30) |
| Primary citation | Palczewski, K.,Kumasaka, T.,Hori, T.,Behnke, C.A.,Motoshima, H.,Fox, B.A.,Le Trong, I.,Teller, D.C.,Okada, T.,Stenkamp, R.E.,Yamamoto, M.,Miyano, M. Crystal structure of rhodopsin: A G protein-coupled receptor. Science, 289:739-745, 2000 Cited by PubMed Abstract: 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. PubMed: 10926528DOI: 10.1126/science.289.5480.739 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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