Figure 2

Overview of the FIV p15 protein. (A) Structure of FIV p15, with the secondary structure elements colored blue-to-red from the N- to the C-terminus and helices numbered h1 to h5. Loops l1 to l4 between the helices are represented as well as the N- and C- termini. (B) Surface representation of the electrostatic properties of FIV p15. The electrostatic potential is shown with positive charges in blue and negative charges in red. The arrow indicates the putative myristoyl-binding pocket of FIV p15. (C) and (D) Docking prediction of the myristoyl insertion in FIV p15 in (C) and out (D) the hydrophobic pocket. The myristoyl group is displayed as a van der Waals representation with gray spheres and its carboxyl functional group in red. The N-terminal glycine residue is represented in magenta. The residues involved in the interaction with the myristoyl group are labeled and displayed in yellow or orange at their initial positions and their positions after the docking experiment, respectively. The backbone of the protein is colored as in (A). (E) The representation of the surface of FIV p15 after docking of the myristoyl group in the external groove. Myristoyl is displayed as in (C) and (D).