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. Author manuscript; available in PMC: 2016 May 24.
Published in final edited form as: Drug Metab Rev. 2012 Dec 5;45(1):79–100. doi: 10.3109/03602532.2012.740049

Figure 3.

Figure 3

(A) Crystal structure of the PXR LBD, with the ligand-binding pocket residues highlighted in magenta. A space-filling model of the binding pocket is shown to better understand the cavity of the pocket. PXR has the unique ability to alter its pocket to allow for the binding of different chemical structures, as exemplified by the pocket volume change from ~1,300 (SR12813 bound) to ~1,600 Å3 (rifampicin bound). (B) Overlay of the SR12813-bound (gray/yellow) and rifampicin-bound (cyan/green) PXR LBDs. Of note is the conformational change required to accommodate the large, macrocyclic compound, rifampicin, which results in three regions in the LBD becoming disordered (yellow). (C) Chemical properties of the residues that surround the ligand-binding pocket. Amino acids are colored to represent the chemical property: orange (hydrophobic); green (polar); blue (basic); red (acidic); yellow (cysteine); and white (glycine).