Slow conformational dynamics of the human A_2A adenosine receptor are temporally ordered.

ABSTRACT: A more complete depiction of protein energy landscapes includes the identification of different function-related conformational states and the determination of the pathways connecting them. We used total internal reflection fluorescence (TIRF) imaging to investigate the conformational dynamics of the human A_2A adenosine receptor (A_2AAR), a class A G protein-coupled receptor (GPCR), at the single-molecule level. Slow, reversible conformational exchange was observed among three different fluorescence emission states populated for agonist-bound A_2AAR. Transitions among these states predominantly occurred in a specific order, and exchange between inactive and active-like conformations proceeded through an intermediate state. Models derived from molecular dynami

SUBMITTER: Wei S 

PROVIDER: S-EPMC8897252 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature