Fig. 4: Drug binding pocket and statin docking.
From: Structure of human drug transporters OATP1B1 and OATP1B3
a Horizontal slice through a ribbon representation of E1S-bound OATP1B1, viewed from the external side, and with E1S shown as orange sticks. TM helices are numbered, and blue and yellow backgrounds depict the N- and C-terminus bundles, respectively. b EM density (blue mesh) of the OATP1B1 with fitted model shown from the membrane plane. Yellow lines indicate potential hydrogen bonds between the sulfate moiety and surrounding residues. Pink line indicates cation-π interaction c Residues within 5 Å of the bound E1S are shown as sticks and labeled. d Molecular lipophilicity potential. Surface representation of the substrate-binding pocket of E1S-bound OATP1B1 and the homology model of OATP1B3 with E17βG docked. Green and yellow indicate more hydrophilic and more hydrophobic areas, respectively. e Close-up views of the representative statin compounds docked in OATP1B1 (blue) and the homology model of OATP1B3 (green) structures using AutoDock Vina37, 38. The fits with the best overall docking scores (values in red) are displayed. Lactone moieties are shaded in orange. Residues for which flexibility of the side chains was allowed during docking are displayed as sticks.
