[Fri-P2-105] Deciphering the ligand binding properties of the mouse odorant-binding protein OBP5 from Mus musculus
- Others:
- Centre des Sciences du Goût et de l'Alimentation [Dijon] (CSGA) ; Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement (INRAE)
- Université Bourgogne Franche-Comté [COMUE] (UBFC)
- Institut de Chimie de Nice (ICN) ; Université Nice Sophia Antipolis (1965 - 2019) (UNS) ; COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA)
- SYstèmes Moléculaires et nanoMatériaux pour l'Energie et la Santé (SYMMES) ; Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG) ; Direction de Recherche Fondamentale (CEA) (DRF (CEA)) ; Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)) ; Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)
Description
Odorant-binding proteins (OBPs) are abundant soluble proteins secreted in the nasal mucus of a variety of species which are believed to be involved in the transport of odorants towards olfactory receptors. In this study, we report the functional characterization of mouse OBP5 (mOBP5). mOBP5 was recombinantly expressed as a hexahistidine-tagged protein in bacteria and purified by metal affinity. Oligomeric state and secondary structure composition of mOBP5 was investigated using gel filtration and circular dichroism spectroscopy. Fluorescent experiments revealed that mOBP5 interacts with the fluorescent probe N-phenyl naphthylamine (NPN) with a micromolar affinity. Competitive binding experiments with 40 odorants indicated that mOBP5 binds a restricted number of odorants with a good affinity. Isothermal titration calorimetry (ITC) confirmed that mOBP5 binds these compounds with association constants in the micromolar range. Finally, protein homology modelling and molecular docking analysis revealed the amino acid residues of mOBP5 guiding its binding properties.
Abstract
International audience
Additional details
- URL
- https://hal.inrae.fr/hal-03810628
- URN
- urn:oai:HAL:hal-03810628v1
- Origin repository
- UNICA