Research Paper Volume 11, Issue 14 pp 5008—5034

Figure 1. Molecular docking analysis shows Ginsenoside Rb1 binding with GABA_A receptor. (A) Original 2D image of Rb1. (B) Modified 3D image of Rb1. (C) Overall map of Rb1 interaction with GABA_ARα1. (D) Interaction between Rb1 with the TMD of GABA_ARα1 receptor. Note that when Rb1 (indicted by green stick) was docked in the TMD of GABA_ARα1, two hydrogen bonds formed with Ile239 and Trp246 sites (indicated by red dotted line). Besides, Rb1 also formed a hydrophobic interaction with multiple hydrophobic amino acids or hydrophobic parts of polar amino acids in the TMD domain of GABA_ARα1 (Ile235, Val238, Ile239, Val243, Trp246, Phe298, Ile302, Ala305, Thr306, Tyr309, Phe310, Ary397, Pro401, Leu402, Phe404) (indicated by blue stick).