Figure 6

In-silico docking of integrase strand transfer inhibitors (INSTIs) at the integrase (IN) active site. The structure of INSTIs L-731,988 (Panel A), S-1360 (B), L-870,812 (C), L-870,810 (D), GS-9137 (E, F) is shown in CPK. The catalytic triad (D64, D116 and E152) is shown in the same color as the protein backbone. Metal ions are presented as yellow balls. Amino acids responsible for drug resistance are colored in magenta. Significant enzyme/ligand interactions are shown as dashed lines (hydrogen bonds in white, metal coordination in yellow, Van-der-Waals forces in red). An adenine (in orange), marking the terminal portion of 3' processed viral DNA has been inserted by superimposition with the indole ring of 5CITEP. The adenine is shown for purely representative reasons, as the docking experiments were conducted in the presence of 5CITEP. A full 3D view of complexes in panels A-E can be obtained using the 3D coordinates provided as additional material [see Additional files 1, 2, 3, 4, 56]. In panel F, superimposition between the IN/inhibitor complex and a crystal structure of RNAse H in complex with an RNA/DNA hybrid results in an overlap between the INSTI (GS-9137 is shown as an example) and the nucleic acid (evidenced in pale green).