Investigation of the conformational dynamics of the A2A adenosine receptor by molecular dynamics simulation

摘要: The structural behavior of the ligand-free form adenosine receptor A2A in an explicit membrane-mimicking environment was investigated by molecular dynamics (MD) simulation. Principal components analysis applied to series MD snapshots and a collection X-ray structures receptor. resulting charts revealed correlation dynamic observed trajectories experimental dataset. most pronounced were intracellular part: TM 5 6 with connecting loop, just as generally recognized crystallographic studies attributed activation. There are grounds for supposing that this pattern intramolecular motions ensues directly from spatial architecture (fold)