1L9H
Crystal structure of bovine rhodopsin at 2.6 angstroms RESOLUTION
1L9H の概要
エントリーDOI | 10.2210/pdb1l9h/pdb |
関連するPDBエントリー | 1F88 1HZX |
分子名称 | rhodopsin, RETINAL, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total) |
機能のキーワード | g protein-coupled receptor, membrane protein, retinal protein, photoreceptor, 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 | 86548.97 |
構造登録者 | Okada, T.,Fujiyoshi, Y.,Silow, M.,Navarro, J.,Landau, E.M.,Shichida, Y. (登録日: 2002-03-23, 公開日: 2002-05-15, 最終更新日: 2024-10-23) |
主引用文献 | Okada, T.,Fujiyoshi, Y.,Silow, M.,Navarro, J.,Landau, E.M.,Shichida, Y. Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography. Proc.Natl.Acad.Sci.USA, 99:5982-5987, 2002 Cited by PubMed Abstract: Activation of G protein-coupled receptors (GPCRs) is triggered and regulated by structural rearrangement of the transmembrane heptahelical bundle containing a number of highly conserved residues. In rhodopsin, a prototypical GPCR, the helical bundle accommodates an intrinsic inverse-agonist 11-cis-retinal, which undergoes photo-isomerization to the all-trans form upon light absorption. Such a trigger by the chromophore corresponds to binding of a diffusible ligand to other GPCRs. Here we have explored the functional role of water molecules in the transmembrane region of bovine rhodopsin by using x-ray diffraction to 2.6 A. The structural model suggests that water molecules, which were observed in the vicinity of highly conserved residues and in the retinal pocket, regulate the activity of rhodopsin-like GPCRs and spectral tuning in visual pigments, respectively. To confirm the physiological relevance of the structural findings, we conducted single-crystal microspectrophotometry on rhodopsin packed in our three-dimensional crystals and show that its spectroscopic properties are similar to those previously found by using bovine rhodopsin in suspension or membrane environment. PubMed: 11972040DOI: 10.1073/pnas.082666399 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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