T
Tetsuji Okada
Researcher at National Institute of Advanced Industrial Science and Technology
Publications - 40
Citations - 10337
Tetsuji Okada is an academic researcher from National Institute of Advanced Industrial Science and Technology. The author has contributed to research in topics: Rhodopsin & G protein-coupled receptor. The author has an hindex of 24, co-authored 35 publications receiving 10017 citations. Previous affiliations of Tetsuji Okada include University of Tokyo & Gakushuin University.
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Journal ArticleDOI
Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
Krzysztof Palczewski,Takashi Kumasaka,Tetsuya Hori,Craig A. Behnke,H. Motoshima,Brian A. Fox,I. Le Trong,David C. Teller,Tetsuji Okada,Ronald E. Stenkamp,Masaki Yamamoto,Masashi Miyano +11 more
TL;DR: This article determined the structure of rhodopsin from diffraction data extending to 2.8 angstroms resolution and found that the highly organized structure in the extracellular region, including a conserved disulfide bridge, forms a basis for the arrangement of the sevenhelix transmembrane motif.
Journal ArticleDOI
The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure
Tetsuji Okada,Minoru Sugihara,Ana-Nicoleta Bondar,Ana-Nicoleta Bondar,Marcus Elstner,Peter Entel,Volker Buss +6 more
TL;DR: A new high-resolution structure is reported for bovine rhodopsin, the visual pigment in rod photoreceptor cells, and a theoretical study of the chromophore geometry has been carried out using combined quantum mechanics/force field molecular dynamics.
Journal ArticleDOI
Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist.
Kazuko Haga,Andrew C. Kruse,Hidetsugu Asada,Takami Yurugi-Kobayashi,Mitsunori Shiroishi,Cheng Zhang,William I. Weis,Tetsuji Okada,Brian K. Kobilka,Tatsuya Haga,Takuya Kobayashi +10 more
TL;DR: The structure of the antagonist-bound human M2 receptor is reported, the first human acetylcholine receptor to be characterized structurally, to the authors' knowledge, and provides insights into the challenges of developing subtype-selective ligands for muscarinic receptors and their propensity for allosteric regulation.
Journal ArticleDOI
Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography.
Tetsuji Okada,Yoshinori Fujiyoshi,Yoshinori Fujiyoshi,Maria Silow,Javier Navarro,Ehud M. Landau,Yoshinori Shichida +6 more
TL;DR: 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.
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Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs).
TL;DR: The further refinement of rhodopsin is described and some clues about how the receptor could be activated by light are provided, to allow models, firmly based on the atomic-resolution structural information, to be further tested as to the conformational changes that these receptors undergo in going from the quiescent to the signaling state.