Propagation of conformational changes during μ-opioid receptor activation

Rémy Sounier, Camille Mas, Jan Steyaert, Toon Laeremans, Aashish Manglik, Weijiao Huang, Brian K. Kobilka, Héléne Déméné () and Sébastien Granier ()
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Rémy Sounier: Institut de Genomique Fonctionnelle, CNRS UMR-5203 INSERM U1191, University of Montpellier
Camille Mas: Institut de Genomique Fonctionnelle, CNRS UMR-5203 INSERM U1191, University of Montpellier
Jan Steyaert: Structural Biology Brussels, Vrije Universiteit Brussel
Toon Laeremans: Structural Biology Brussels, Vrije Universiteit Brussel
Aashish Manglik: Stanford University School of Medicine
Weijiao Huang: Stanford University School of Medicine
Brian K. Kobilka: Stanford University School of Medicine
Héléne Déméné: Centre de Biochimie Structurale, CNRS UMR 5048-INSERM 1054- University of Montpellier
Sébastien Granier: Institut de Genomique Fonctionnelle, CNRS UMR-5203 INSERM U1191, University of Montpellier

Nature, 2015, vol. 524, issue 7565, 375-378

Abstract: NMR spectroscopy reveals the conformational changes of the μ-opioid receptor that are associated with receptor activation, helping to explain why the allosteric coupling between the agonist-binding pocket and the cytoplasmic G-protein-coupling interface of this receptor is relatively weak.

Date: 2015
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DOI: 10.1038/nature14680

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