Figure 3
From: Molecular basis for the recognition of 24-(S)-hydroxycholesterol by integrin αvβ3
Molecular interactions of 24HC at site II of integrin αvβ3. (A) Molecular docking and MD simulations revealed that 24HC binds to integrin αvβ3 at site II in an orientation that is distinct from that of 25HC. In this orientation, the 3-OH group engages in polar interactions with S162 and A263 of the βI domain, and the 24-OH group is near S399 of the β-propeller domain. The two domains of integrin αvβ3 are shown as secondary structure representation, and the binding site residues are shown in licorice. (B) The distance between the center-of-mass (COM) of the binding site residues and COM of 24HC through the entire simulation time (200 ns) indicates the stability of the ligand within the binding site. (C) Major polar interactions between the two hydroxyl groups of 24HC and various binding site residues are tracked as distances between the interacting functional groups. (D–E) Radar charts showing the polar and hydrophobic interactions between 24HC and various binding site residues quantified as % occupancy, the fraction of the simulation time during which 24HC is within 5 Å of the listed residues from the β-propeller domain (light green), and the βI domain (light pink), respectively.
