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Figure 4.
Figure 4. The mRXRαF318A Ligand-Binding Pocket(A) Oleic
acid (OA) interactions with the mRXRαF318A LBD. Interactions
between the protein and the ligand (4.2 Å cutoff) are
depicted as broken lines. Residue names are colored as a
function of the mRXRαF318A structural element from which they
originate. W indicates a water molecule.(B) Stereo view of the
2.5 Å resolution (2F[o]-F[c]) map contoured at 1.0
standard deviation, with OA docked into its binding site. The
protein Cα trace is represented in gray, the contacting side
chains (carbons, yellow; oxygen, red; nitrogen, blue; sulphur,
green) and the ligand (blue) by thick lines.(C) Superposition of
the ligand-binding sites of the mRXRαF318A/OA (blue) and the
hRXRα/9C-RA (pink) LBDs. The gray arrows highlight the
different ligand-specific induced conformations in both
complexes. Helices (ribbons) and loops (rods) are indicated, as
well as some residues (mouse RXRα numbering) discussed in the
text.
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