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. Author manuscript; available in PMC: 2017 Dec 1.
Published in final edited form as: Biochim Biophys Acta. 2016 Sep 3;1864(12):1667–1677. doi: 10.1016/j.bbapap.2016.08.019

Fig. 6. Visualization of human FXR-LBD prenylflavonoid interactions.

Fig. 6

A, Ribbon representation of the co-crystal structure of FXR-LBD bound to 3-deoxy-CDCA complex, PDB 1OT7, with the Trp residues at positions 454 and 469 displayed as sticks and colored in blue. Arrows mark the approximate positions of the residues, R331, S332, and Y 369, for which interactions were predicted with the prenylflavonoid ligands. The N-terminal region (201–241) is not visible in PDB 1OT7. Docking models of B, XN, C, TX, D, IX, and E, 8PN into human FXR-LBD (Molsoft ICM). Computational molecular docking predicts and identifies non-covalent interactions established between ligands and protein. Docked ligands are displayed as sticks and colored by atom type, with carbon atoms in magenta (XN), orange (TX), cyan (IX) and white (8PN); protein residues are displayed as stick with the carbon atoms colored in green. Secondary structure is displayed as ribbon. Protein-ligand hydrogen binding interactions are displayed as dashed black lines. The docking models do not encompass the N-terminal region 201–241.