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Crystal structure of metarhodopsin II

Author

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  • Hui-Woog Choe

    (Institut für Medizinische Physik und Biophysik - CC2, Charité - Universitätsmedizin Berlin, Charitéplatz 1
    College of Natural Science, Chonbuk National University)

  • Yong Ju Kim

    (Institut für Medizinische Physik und Biophysik - CC2, Charité - Universitätsmedizin Berlin, Charitéplatz 1)

  • Jung Hee Park

    (Institut für Medizinische Physik und Biophysik - CC2, Charité - Universitätsmedizin Berlin, Charitéplatz 1)

  • Takefumi Morizumi

    (Institut für Medizinische Physik und Biophysik - CC2, Charité - Universitätsmedizin Berlin, Charitéplatz 1
    Present addresses: Department of Biochemistry, University of Toronto, 1 King’s College Circle, Toronto, Ontario M5S 1A8, Canada (T.M.); Departments of Biochemistry and Molecular Genetics, University of Toronto, 1 King’s College Circle, Toronto, Ontario M5S 1A8, Canada (O.P.E.).)

  • Emil F. Pai

    (Molecular Genetics and Medical Biophysics, University of Toronto, 1 King’s College Circle)

  • Norbert Krauß

    (Queen Mary University of London, School of Biological and Chemical Sciences)

  • Klaus Peter Hofmann

    (Institut für Medizinische Physik und Biophysik - CC2, Charité - Universitätsmedizin Berlin, Charitéplatz 1
    Zentrum für Biophysik und Bioinformatik, Humboldt-Universität zu Berlin, Invalidenstrasse 42)

  • Patrick Scheerer

    (Institut für Medizinische Physik und Biophysik - CC2, Charité - Universitätsmedizin Berlin, Charitéplatz 1)

  • Oliver P. Ernst

    (Institut für Medizinische Physik und Biophysik - CC2, Charité - Universitätsmedizin Berlin, Charitéplatz 1
    Present addresses: Department of Biochemistry, University of Toronto, 1 King’s College Circle, Toronto, Ontario M5S 1A8, Canada (T.M.); Departments of Biochemistry and Molecular Genetics, University of Toronto, 1 King’s College Circle, Toronto, Ontario M5S 1A8, Canada (O.P.E.).)

Abstract

Rhodopsin activation Structural studies of active states of the visual pigment rhodopsin, a G protein-coupled receptor, have previously been limited to apoprotein or opsin forms that do not contain the agonist all-trans-retinal. Two groups now report structures that reveal more details of the transformations involved in rhodopsin activation. Choe et al. solve the X-ray crystal structure of the metarhodopsin II intermediate of the photoreceptor rhodopsin, and Standfuss et al. determine the structure of a constitutively active mutant of rhodopsin bound to a peptide derived from the C-terminus of the G protein transducin.

Suggested Citation

  • Hui-Woog Choe & Yong Ju Kim & Jung Hee Park & Takefumi Morizumi & Emil F. Pai & Norbert Krauß & Klaus Peter Hofmann & Patrick Scheerer & Oliver P. Ernst, 2011. "Crystal structure of metarhodopsin II," Nature, Nature, vol. 471(7340), pages 651-655, March.
    • Handle: RePEc:nat:nature:v:471:y:2011:i:7340:d:10.1038_nature09789
    DOI: 10.1038/nature09789
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    Cited by:

    1. Arum Wu & David Salom & John D. Hong & Aleksander Tworak & Kohei Watanabe & Els Pardon & Jan Steyaert & Hideki Kandori & Kota Katayama & Philip D. Kiser & Krzysztof Palczewski, 2023. "Structural basis for the allosteric modulation of rhodopsin by nanobody binding to its extracellular domain," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    2. Yuxia Qian & Jiening Wang & Linlin Yang & Yanru Liu & Lina Wang & Wei Liu & Yun Lin & Hong Yang & Lixin Ma & Sheng Ye & Shan Wu & Anna Qiao, 2022. "Activation and signaling mechanism revealed by GPR119-Gs complex structures," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    3. Takashi Sasaki & Moeko Mita & Naho Ikari & Ayane Kuboyama & Shuzo Hashimoto & Tatsuya Kaneko & Masaji Ishiguro & Makoto Shimizu & Jun Inoue & Ryuichiro Sato, 2017. "Identification of key amino acid residues in the hTGR5–nomilin interaction and construction of its binding model," PLOS ONE, Public Library of Science, vol. 12(6), pages 1-15, June.

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