1F88

CRYSTAL STRUCTURE OF BOVINE RHODOPSIN

1F88 の概要

• エントリーDOI: 10.2210/pdb1f88/pdb
• 分子名称: 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)
• 機能のキーワード: photoreceptor, g protein-coupled receptor, membrane protein, retinal protein, visual pigment, signaling protein
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Membrane; Multi-pass membrane protein: P02699
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81956.71

構造登録者

Okada, T.,Palczewski, K.,Stenkamp, R.E.,Miyano, M. (登録日: 2000-06-29, 公開日: 2000-08-04, 最終更新日: 2024-10-30)

主引用文献

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

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: 10926528
DOI: 10.1126/science.289.5480.739

実験手法

X-RAY DIFFRACTION (2.8 Å)