9.A.14.3.5
β-2 adrenergic receptor, β2-AR. Activates adenylate cyclase through G proteins. Binds epinephrine with 30x greater affinity than norepenephrine.  Functions as an ATP-independent phospholipid flippase (scramblase) (Goren et al. 2014). A parameterized MARTINI program can be used to predict the hinging motions of the protein (Li et al. 2019). The drugs, salmeterol, formoterol and salbutamol, constitute the frontline treatment for asthma and other chronic pulmonary diseases. These drugs activate beta2-AR, and differ significantly in their clinical onset and durations of actions. Membrane lipids facilitate access and binding of the ligands, affecting their molecular recognition and pharmacology (Szlenk et al. 2021).  Fullerene and fullerene derivatives affect the local structure of beta2AR, especially the distortion of helix4, but bring about no great changes within the overall structure (Li et al. 2019). The drugs, salmeterol, formoterol and salbutamol, constitute the frontline treatment for asthma and other chronic pulmonary diseases. These drugs activate beta2-AR, and differ significantly in their clinical onset and durations of actions. Membrane lipids facilitate access and binding of the ligands, affecting their molecular recognition and pharmacology (Szlenk et al. 2021).  Fullerene and fullerene derivatives affect the local structure of beta2AR, especially the distortion of helix4, but bring about no great changes within the overall structure (Ren et al. 2022).