caa a22 4500 445325720 CHVBK 20180317142719.0 cr unu---uuuuu 170323e20110701xx s 000 0 eng 10.1007/s10858-011-9523-3 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9523-3 Electrostatically-driven fast association and perdeuteration allow detection of transferred cross-relaxation for G protein-coupled receptor ligands with equilibrium dissociation constants in the high-to-low nanomolar range [Elektronische Daten] [Laurent Catoire, Marjorie Damian, Marc Baaden, Éric Guittet, Jean-Louis Banères] The mechanism of signal transduction mediated by G protein-coupled receptors is a subject of intense research in pharmacological and structural biology. Ligand association to the receptor constitutes a critical event in the activation process. Solution-state NMR can be amenable to high-resolution structure determination of agonist molecules in their receptor-bound state by detecting dipolar interactions in a transferred mode, even with equilibrium dissociation constants below the micromolar range. This is possible in the case of an inherent ultra-fast diffusive association of charged ligands onto a highly charged extracellular surface, and by slowing down the 1H-1H cross-relaxation by perdeuterating the receptor. Here, we demonstrate this for two fatty acid molecules in interaction with the leukotriene BLT2 receptor, for which both ligands display a submicromolar affinity. Springer Science+Business Media B.V., 2011 Kinetics nationallicence Transferred NOE nationallicence G protein-coupled receptor nationallicence Signal transduction nationallicence Structural biology nationallicence Catoire Laurent Laboratoire de Biologie Physico-Chimique des Protéines Membranaires, UMR 7099 CNRS/Université Paris-7, Institut de Biologie Physico-Chimique (FRC 550), 13 rue Pierre et Marie Curie, 75005, Paris, France aut Damian Marjorie Institut des Biomolécules Max Mousseron, UMR 5247 CNRS, Université Montpellier 1 and Université Montpellier 2, 15 Avenue C. Flahault, 34093, Montpellier, France aut Baaden Marc Laboratoire de Biochimie Théorique, UPR 9080 CNRS/Université Paris-7, Institut de Biologie Physico-Chimique (FRC 550), 13 rue Pierre et Marie Curie, 75005, Paris, France aut Guittet Éric Centre de Recherche de Gif, Laboratoire de Chimie et Biologie Structurales, ICSN, UPR 2301 CNRS, 91198, Gif-sur-Yvette, France aut Banères Jean-Louis Institut des Biomolécules Max Mousseron, UMR 5247 CNRS, Université Montpellier 1 and Université Montpellier 2, 15 Avenue C. Flahault, 34093, Montpellier, France aut Journal of Biomolecular NMR Springer Netherlands 50/3(2011-07-01), 191-195 0925-2738 50:3<191 2011 50 10858 https://doi.org/10.1007/s10858-011-9523-3 text/html Onlinezugriff via DOI 1 brief-communication jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9523-3 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Catoire Laurent Laboratoire de Biologie Physico-Chimique des Protéines Membranaires, UMR 7099 CNRS/Université Paris-7, Institut de Biologie Physico-Chimique (FRC 550), 13 rue Pierre et Marie Curie, 75005, Paris, France aut NATIONALLICENCE 700 1- Damian Marjorie Institut des Biomolécules Max Mousseron, UMR 5247 CNRS, Université Montpellier 1 and Université Montpellier 2, 15 Avenue C. Flahault, 34093, Montpellier, France aut NATIONALLICENCE 700 1- Baaden Marc Laboratoire de Biochimie Théorique, UPR 9080 CNRS/Université Paris-7, Institut de Biologie Physico-Chimique (FRC 550), 13 rue Pierre et Marie Curie, 75005, Paris, France aut NATIONALLICENCE 700 1- Guittet Éric Centre de Recherche de Gif, Laboratoire de Chimie et Biologie Structurales, ICSN, UPR 2301 CNRS, 91198, Gif-sur-Yvette, France aut NATIONALLICENCE 700 1- Banères Jean-Louis Institut des Biomolécules Max Mousseron, UMR 5247 CNRS, Université Montpellier 1 and Université Montpellier 2, 15 Avenue C. Flahault, 34093, Montpellier, France aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 50/3(2011-07-01), 191-195 0925-2738 50:3<191 2011 50 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer