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- Krzysztof Palczewski
- Department of Ophthalmology,
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- Takashi Kumasaka
- Structural Biophysics Laboratory, RIKEN Harima Institute, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan.
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- Tetsuya Hori
- Structural Biophysics Laboratory, RIKEN Harima Institute, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan.
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- Craig A. Behnke
- Department of Biochemistry,
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- Hiroyuki Motoshima
- Structural Biophysics Laboratory, RIKEN Harima Institute, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan.
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- Brian A. Fox
- Department of Biochemistry,
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- Isolde Le Trong
- Department of Biological Structure, and
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- David C. Teller
- Department of Biochemistry,
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- Tetsuji Okada
- Department of Ophthalmology,
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- Ronald E. Stenkamp
- Department of Biological Structure, and
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- Masaki Yamamoto
- Structural Biophysics Laboratory, RIKEN Harima Institute, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan.
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- Masashi Miyano
- Structural Biophysics Laboratory, RIKEN Harima Institute, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan.
書誌事項
- 公開日
- 2000-08-04
- DOI
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- 10.1126/science.289.5480.739
- 公開者
- American Association for the Advancement of Science (AAAS)
この論文をさがす
説明
<jats:p> 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 α 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- <jats:italic>cis</jats:italic> -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. </jats:p>
収録刊行物
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- Science
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Science 289 (5480), 739-745, 2000-08-04
American Association for the Advancement of Science (AAAS)