Probing thermostability of detergent-solubilized CB₂ receptor by parallel G protein-activation and ligand-binding assays.

ABSTRACT: G protein-coupled receptors (GPCRs) comprise a large class of integral membrane proteins involved in the regulation of a broad spectrum of physiological processes and are a major target for pharmaceutical drug development. Structural studies can help advance the rational design of novel specific pharmaceuticals that target GPCRs, but such studies require expression of significant quantities of these proteins in pure, homogenous, and sufficiently stable form. An essential precursor for these structural studies is an assessment of protein stability under experimental conditions. Here we report that solubilization of a GPCR, type II cannabinoid receptor CB₂, in a Façade detergent enables radioligand thermostability assessments of this receptor with low background from nonspecific i

SUBMITTER: Beckner RL 

PROVIDER: S-EPMC6952600 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature