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Crystal structure of the ligand-free G-protein-coupled receptor opsin

Author

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  • Jung Hee Park

    (Institut für Medizinische Physik und Biophysik (CC2), Charité–Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany)

  • Patrick Scheerer

    (Institut für Medizinische Physik und Biophysik (CC2), Charité–Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany)

  • Klaus Peter Hofmann

    (Institut für Medizinische Physik und Biophysik (CC2), Charité–Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany
    Zentrum für Biophysik und Bioinformatik, Humboldt-Universität zu Berlin, Invalidenstrasse 42, D-10115 Berlin, Germany)

  • Hui-Woog Choe

    (Institut für Medizinische Physik und Biophysik (CC2), Charité–Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany
    College of Natural Science, Chonbuk National University)

  • Oliver Peter Ernst

    (Institut für Medizinische Physik und Biophysik (CC2), Charité–Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany)

Abstract

In the G-protein-coupled receptor (GPCR) rhodopsin, the inactivating ligand 11-cis-retinal is bound in the seven-transmembrane helix (TM) bundle and is cis/trans isomerized by light to form active metarhodopsin II. With metarhodopsin II decay, all-trans-retinal is released, and opsin is reloaded with new 11-cis-retinal. Here we present the crystal structure of ligand-free native opsin from bovine retinal rod cells at 2.9 ångström (Å) resolution. Compared to rhodopsin, opsin shows prominent structural changes in the conserved E(D)RY and NPxxY(x)5,6F regions and in TM5–TM7. At the cytoplasmic side, TM6 is tilted outwards by 6–7 Å, whereas the helix structure of TM5 is more elongated and close to TM6. These structural changes, some of which were attributed to an active GPCR state, reorganize the empty retinal-binding pocket to disclose two openings that may serve the entry and exit of retinal. The opsin structure sheds new light on ligand binding to GPCRs and on GPCR activation.

Suggested Citation

  • Jung Hee Park & Patrick Scheerer & Klaus Peter Hofmann & Hui-Woog Choe & Oliver Peter Ernst, 2008. "Crystal structure of the ligand-free G-protein-coupled receptor opsin," Nature, Nature, vol. 454(7201), pages 183-187, July.
    • Handle: RePEc:nat:nature:v:454:y:2008:i:7201:d:10.1038_nature07063
    DOI: 10.1038/nature07063
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    Cited by:

    1. Valérie Capra & Marta Busnelli & Alessandro Perenna & Manuela Ambrosio & Maria Rosa Accomazzo & Celine Galés & Bice Chini & G Enrico Rovati, 2013. "Full and Partial Agonists of Thromboxane Prostanoid Receptor Unveil Fine Tuning of Receptor Superactive Conformation and G Protein Activation," PLOS ONE, Public Library of Science, vol. 8(3), pages 1-12, March.

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