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. Author manuscript; available in PMC: 2012 Dec 7.
Published in final edited form as: Arch Biochem Biophys. 2010 Aug 1;504(1):11–16. doi: 10.1016/j.abb.2010.07.025

Figure 3. Docking of β-apo-13-carotenone with the RXRα tetramer.

Figure 3

Shown is the structure of the ligand-binding domain of the tetrameric RXRα (in green) from PDB entry 1G5Y with: (a) the bound crystallized all-trans retinoic acid (ATRA) isomer (in white) and the Surfle-Dock docked structure of β-apo-13-carotenone (yellow) when built in a conformation resembling that of the bound ATRA; (b) same as in (a) with the protein helix 3 removed to facilitate visualization of the quality of docking in the binding site; (c) as in (a) with the RXR protein removed to show details of the similarity of the crystallized ATRA ligand and the docked pose of β-apo-13-carotenone.