Fig. 6: GaMD simulations of Gi activation by dexmedetomidine-bound α2A-AR.
From: Distinct binding conformations of epinephrine with α- and β-adrenergic receptors
a Diagram showing the GDP-binding pocket of Gαi. Ionic and hydrogen bonds are depicted as dashed black lines. b E43 interacts with R178 in the inactive GDP-bound Gαi. c K46 interacts with D200 in nucleotide-free Gαi. Ionic and hydrogen bonds are depicted as dashed black lines. d, e The distance between K46 and D200 of Gαi calculated from the GaMD simulations when Gi is bound to GDP (d) or is nucleotide free (e). f, g The distance between the Ras-like domain and the α-helical domain of Gαi calculated from the GaMD simulations when Gi is bound to GDP (f) or is nucleotide free (g). (h, i) The distance between K192 and D341 of Gαi calculated from the GaMD simulations when Gi is bound to GDP (h) or is nucleotide free (i). j, k The distance between Q52 and A326 of Gαi calculated from the GaMD simulations when Gi is bound to GDP (j) or is nucleotide free (k). l, m The distance between E43 and R178 of Gαi calculated from the GaMD simulations when Gi is bound with GDP (l) or is nucleotide-free (m). Four independent 3000 ns GaMD simulations are shown for each condition.
