Abstract

G protein-coupled receptors (GPCRs) regulate numerous physiological processes and are key therapeutic targets. While class A GPCRs can function as monomers, evidence suggests they can also form dimers or higher-order oligomers, potentially influencing their function. The mu-opioid (MOR) and cannabinoid CB1 receptors, both involved in pain signaling, have been suggested to interact. Thus, we investigated the dimerization between MOR and CB1 receptors through CG MD simulations and we identified key contacts at the interfaces and analyzed mutations at these residues with confocal microscopy and cAMP accumulation assays. This dataset provides raw data underlying the confocal microscope analysis, cAMP ELISA assays, and flow cytometry experiments described in the associated manuscript. Data were generated within the framework of Horizon 2020 project “QSPainRelief” and are presented as seven spreadsheets.