Published 2022
| Version v1
Journal article
The Third Extracellular Loop of Mammalian Odorant Receptors Is Involved in Ligand Binding
Contributors
Others:
- Daegu Gyeongbuk Institute of Science and Technology (DGIST)
- Institut de Chimie de Nice (ICN) ; Université Nice Sophia Antipolis (1965 - 2019) (UNS)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UniCA)
- Institut de Génomique Fonctionnelle (IGF) ; Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)
- In this work, J.P was supported by the Fondation Roudnitska under the aegis of Fondation de France and C.M was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (2020R1A6A1A03040516 and 2020R1A2C2005174)
Description
Mammals recognize chemicals in the air via G protein-coupled odorant receptors (ORs). In addition to their orthosteric binding site, other segments of these receptors modulate ligand recognition. Focusing on human hOR1A1, which is considered prototypical of class II ORs, we used a combination of molecular modeling, site-directed mutagenesis, and in vitro functional assays. We showed that the third extracellular loop of ORs (ECL3) contributes to ligand recognition and receptor activation. Indeed, site-directed mutations in ECL3 showed differential effects on the potency and efficacy of both carvones, citronellol, and 2-nonanone.
Abstract
International audienceAdditional details
Identifiers
- URL
- https://hal.science/hal-04712540
- URN
- urn:oai:HAL:hal-04712540v1
Origin repository
- Origin repository
- UNICA