Figure 2.
Fig. 2. Three experimentally observed positions of SR12813 in
the ligand-binding pocket of hPXR. Intermolecular interactions
are shown with amino acid side chains in blue and the C atom as a
sphere. The positions 1, 2, and 3 of SR12813 are rendered in
cyan, purple, and orange, respectively. Equivalent side chains
from the apo structure are shown in white. A small number of
residues undergo rotamer shifts (Met243, Cys284, and His407) or
small shifts in position (Ser208 and Leu209) upon SR12813
binding. Residues mutated to examine the specificity of mouse
PXR are underlined. (A) Position 1 makes van der Waals contacts
with eight side chains, and forms one 3.0 Å hydrogen bond
with Ser247. (B) Position 2 makes van der Waals contacts with
seven side chains, and forms one 2.8 Å hydrogen bond with
His407. (C) Position 3 makes van der Waals contacts with six
side chains, and forms three hydrogen bonds with Ser247, Gln285,
and Ser208, which forms a water-mediated hydrogen bond. See also
Web table 2 and Web fig. 2 (25).
atom as a
sphere. The positions 1, 2, and 3 of SR12813 are rendered in
cyan, purple, and orange, respectively. Equivalent side chains
from the apo structure are shown in white. A small number of
residues undergo rotamer shifts (Met243, Cys284, and His407) or
small shifts in position (Ser208 and Leu209) upon SR12813
binding. Residues mutated to examine the specificity of mouse
PXR are underlined. (A) Position 1 makes van der Waals contacts
with eight side chains, and forms one 3.0 Å hydrogen bond
with Ser247. (B) Position 2 makes van der Waals contacts with
seven side chains, and forms one 2.8 Å hydrogen bond with
His407. (C) Position 3 makes van der Waals contacts with six
side chains, and forms three hydrogen bonds with Ser247, Gln285,
and Ser208, which forms a water-mediated hydrogen bond. See also
Web table 2 and Web fig. 2 (25).