أعرض في EDS

Structure and dynamics of G protein-coupled receptor–bound ghrelin reveal the critical role of the octanoyl chain

التفاصيل البيبلوغرافية
العنوان: Structure and dynamics of G protein-coupled receptor–bound ghrelin reveal the critical role of the octanoyl chain
المؤلفون: Pascal Demange, Maxime Louet, Alain Milon, Jacky Marie, Guillaume Ferré, Georges Czaplicki, Jean-Louis Banères, Pedro Renault, Laurent Gavara, Nicolas Floquet, Céline M'Kadmi, Sonia Cantel, Jean-Alain Fehrentz, Bartholomé Delort, Oliver Saurel, Marjorie Damian
المساهمون: Laboratoire de l'intégration, du matériau au système (IMS), Université Sciences et Technologies - Bordeaux 1-Institut Polytechnique de Bordeaux-Centre National de la Recherche Scientifique (CNRS), Molécules Thérapeutiques in silico (MTI), Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de pharmacologie et de biologie structurale (IPBS), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS), Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Synthèse et étude de systèmes à intêret biologique (SEESIB), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Groupe de recherche et d'analyse du social et de la sociabilité (GRASS), Université Paris 8 Vincennes-Saint-Denis (UP8)-Centre National de la Recherche Scientifique (CNRS), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Université Sciences et Technologies - Bordeaux 1 (UB)-Institut Polytechnique de Bordeaux-Centre National de la Recherche Scientifique (CNRS), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), ANR-17-CE11-0011,allosig,allostérie, dynamique conformationnelle et signalisation via les RCPG(2017)
المصدر: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (35), pp.17525-17530. ⟨10.1073/pnas.1905105116⟩
Proceedings of the National Academy of Sciences of the United States of America, 2019, 116 (35), pp.17525-17530. ⟨10.1073/pnas.1905105116⟩
بيانات النشر: HAL CCSD, 2019.
سنة النشر: 2019
مصطلحات موضوعية: Models, Molecular, 0301 basic medicine, Agonist, Conformational change, Magnetic Resonance Spectroscopy, Molecular model, Protein Conformation, medicine.drug_class, Acylation, [SDV]Life Sciences [q-bio], Growth hormone secretagogue receptor, Peptide, 010402 general chemistry, 01 natural sciences, Receptors, G-Protein-Coupled, Structure-Activity Relationship, 03 medical and health sciences, medicine, Animals, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Receptor, ComputingMilieux_MISCELLANEOUS, G protein-coupled receptor, chemistry.chemical_classification, Binding Sites, Multidisciplinary, digestive, oral, and skin physiology, Biological Sciences, Ghrelin, 0104 chemical sciences, [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, 030104 developmental biology, chemistry, Biophysics, hormones, hormone substitutes, and hormone antagonists, Protein Binding, Signal Transduction
الوصف: Ghrelin plays a central role in controlling major biological processes. As for other G protein-coupled receptor (GPCR) peptide agonists, the structure and dynamics of ghrelin bound to its receptor remain obscure. Using a combination of solution-state NMR and molecular modeling, we demonstrate that binding to the growth hormone secretagogue receptor is accompanied by a conformational change in ghrelin that structures its central region, involving the formation of a well-defined hydrophobic core. By comparing its acylated and nonacylated forms, we conclude that the ghrelin octanoyl chain is essential to form the hydrophobic core and promote access of ghrelin to the receptor ligand-binding pocket. The combination of coarse-grained molecular dynamics studies and NMR should prove useful in improving our mechanistic understanding of the complex conformational space explored by a natural peptide agonist when binding to its GPCR. Such information should also facilitate the design of new ghrelin receptor-selective drugs.
اللغة: English
تدمد: 0027-8424
1091-6490
DOI: 10.1073/pnas.1905105116⟩
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbbcacfa3f0afdf98c0d03a456af2291
https://hal.archives-ouvertes.fr/hal-02322092
Rights: OPEN
رقم الانضمام: edsair.doi.dedup.....dbbcacfa3f0afdf98c0d03a456af2291
قاعدة البيانات: OpenAIRE
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IllustrationInfo