Ligand modulation of the conformational dynamics of the A_2A adenosine receptor revealed by single-molecule fluorescence.

ABSTRACT: G protein-coupled receptors (GPCRs) are the largest class of transmembrane proteins, making them an important target for therapeutics. Activation of these receptors is modulated by orthosteric ligands, which stabilize one or several states within a complex conformational ensemble. The intra- and inter-state dynamics, however, is not well documented. Here, we used single-molecule fluorescence to measure ligand-modulated conformational dynamics of the adenosine A_2A receptor (A_2AR) on nanosecond to millisecond timescales. Experiments were performed on detergent-purified A₂R in either the ligand-free (apo) state, or when bound to an inverse, partial or full agonist ligand. Single-molecule Förster resonance energy transfer (smFRET) was performed on detergent-sol

SUBMITTER: Fernandes DD 

PROVIDER: S-EPMC7960716 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature