Fig. 5: Characterization of the binding pocket of OATP1B1 and OATP1B3.
From: Structure of human drug transporters OATP1B1 and OATP1B3
a Road-kill plot presenting the interaction between bound E1S and the residues of OATP1B1. Hydrogen bonds are depicted as pink dotted lines. Cation-π interaction is shown as orange line. TM helices and interacting residues are labeled. b Electrostatic surface potential of the binding pocket of OATP1B1 and homology model of OATP1B3. Blue and red indicate positive and negative charges, respectively. White indicates neutral residues. c Molecular docking of E1S in OATP1B1 and E17βG in the homology model of OATP1B3 using AutoDock Vina37, 38. The fits with the best overall docking score are displayed (the best three fits are illustrated for E1S). E1S-bound structure (left) is displayed for comparison. Eight residues, for which flexibility was allowed in the molecular docking, are displayed at sticks. The residues of interest in both OATP1B1 and OATP1B3 and labeled.
