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. Author manuscript; available in PMC: 2016 Apr 1.
Published in final edited form as: Toxicol Appl Pharmacol. 2015 Feb 10;284(1):54–64. doi: 10.1016/j.taap.2015.02.001

Figure 3. Alignment of hPXR and pbPXR supplemented with known secondary structure and ligand-binding residues.

Figure 3

Human PXR structures (Chrencik et al. 2005; Teotico et al. 2008; Watkins et al. 2001; Watkins et al. 2003; Xue et al. 2007a; Xue et al. 2007b) was used to supplement a hPRX and pbPXR amino acid sequence comparison with information of residues known to be involved in ligand binding, secondary structures, salt bridge and SRC-1 interaction. Rectangular boxes indicate α-helices (α) and arrows anti β-strands that form an antiparallel (AP) sheet. Stars indicate ligand-binding residues, squares residues involved in salt-bridges and triangles residues interacting with co-activator (SRC-1).