Structural and Functional Characterization of Human Peripheral Nervous System Myelin Protein P2
Figure 6
Identification of cholesterol as a potential ligand for P2.
A. Structure of the more favourable complex of P2 protein with cholesterol (green), obtained by the docking simulations. The position of the palmitate (orange) found in the crystal is shown for comparison. The polar heads of the two ligands are coloured by element. The favourable interactions formed at the binding site with Arg106, Arg126, and Tyr128 residues (in sticks) are shown as black lines. The main hydrophobic contact residues are also shown. Inset: Structure of the more favourable complex of P2 with palmitate (green), obtained by the docking simulations. The position of the palmitate (blue) as found in the crystal is shown also. Arg106, Arg126, and Tyr128 and their favourable interactions with the two ligands are shown. B. Emission fluorescence spectra of a) human P2 9.4 µM and b) human P2 9.4 µM plus cholesterol 10 µM after 120 min of incubation at room temperature.