Insights into adenosine A2A receptor activation through cooperative modulation of agonist and allosteric lipid interactions.

ABSTRACT: The activation process of G protein-coupled receptors (GPCRs) has been extensively studied, both experimentally and computationally. In particular, Molecular Dynamics (MD) simulations have proven useful in exploring GPCR conformational space. The typical behaviour of class A GPCRs, when subjected to unbiased MD simulations from their crystallized inactive state, is to fluctuate between inactive and intermediate(s) conformations, even with bound agonist. Fully active conformation(s) are rarely stabilized unless a G protein is also bound. Despite several crystal structures of the adenosine A2a receptor (A2aR) having been resolved in complex with co-crystallized agonists and Gs protein, its agonist-mediated activation process is still not completely understood. In order to thoroughly examine

SUBMITTER: Bruzzese A 

PROVIDER: S-EPMC7188303 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature