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How broadly tuned olfactory receptors equally recognize their agonists. Human OR1G1 as a test case |
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| Authors: | Landry Charlier Jérémie Topin Catherine Ronin Soo-Kyung Kim William A Goddard III Roman Efremov Jér?me Golebiowski |
| Institution: | 1. Institut de Chimie de Nice, UMR CNRS, Université de Nice Sophia Antipolis 7272, 06108, Nice Cedex 2, France 5. Institut des Biomolécules Max Mousseron, CNRS-UMR 5247, Faculté de Pharmacie, Université Montpellier 1, Université Montpellier 2, 15 Avenue Charles Flahault, BP 14491, 34093, Montpellier Cedex 5, France 2. Laboratoire de Neuroglycobiologie, GLM, CNRS, 31 Ch. J. Aiguier, 13402, Marseille, France 3. Materials and Process Simulation Center (MC139-74), California Institute of Technology, 1200 E. California Blvd., Pasadena, CA, 91125, USA 4. Laboratory of Biomolecular Modeling, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ul. Miklukho-Maklaya, 16/10, 117997, Moscow, Russia |
| Abstract: | The molecular features that dominate the binding mode of agonists by a broadly tuned olfactory receptor are analyzed through a joint approach combining cell biology, calcium imaging, and molecular modeling. The odorant/receptor affinities, estimated through statistics accrued during molecular dynamics simulations, are in accordance with the experimental ranking. Although in many systems receptors recognize their target through a network of oriented interactions, such as H-bonding, the binding by broadly tuned olfactory receptors is dominated by non-polar terms. We show how such a feature allows chemicals belonging to different chemical families to similarly activate the receptors through compensations of interactions within the binding site. |
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