Fig. 2: Interactions between epinephrine and α2A-AR.
From: Distinct binding conformations of epinephrine with α- and β-adrenergic receptors
a Schematic diagram of the epinephrine-binding pocket of α2A-AR from the cryo-EM structure. Hydrogen bonds are depicted as dashed black lines. b–f Time courses of the interactions between epinephrine and specific residues of α2A-AR were calculated from the GaMD simulations: the distance between the CG atom of D128 and the N1 atom of epinephrine (b), the CG atom of D128 and the O3 atoms of epinephrine (c), the OH atom of Y431 and the N1 atom of epinephrine (d), the OG atom of S215 and the O1 atom of epinephrine (e), the OG atom of S219 and the O2 atom of epinephrine (f), and the phenyl group of F427 and the methyl group of epinephrine (g). h Functional studies of the epinephrine-interacting residues of α2A-AR. The effects of wild-type and mutant α2A-AR on the cAMP inhibition signaling initiated by epinephrine were studied. The data are shown as the means ± SDs of three independent experiments.
