Evolutionary plasticity of SH3 domain binding by Nef proteins of the HIV-1/SIVcpz lentiviral lineage
Fig 2
HIV-1 M consensus Nef amino acid sequence (A) and an alignment of the conserved central region (underlined in A) of selected Nef proteins from different primate lentiviruses (B). The key residues of the core SH3 docking site (PxxPxR motif), including R77, are highlighted in light blue. Residues involved in a binding pocket for the Hck SH3 domain RT-loop that are conserved in HIV-1 and HIV-1-like Nef proteins are highlighted in yellow. Residues at positions 83 and 120 forming the R-clamp coordinating the positioning of R77 are shown in bold and colored according to their side chain properties (small in green, hydrophilic in blue, aliphatic or methionine in red, aromatic in brown). The names of HIV/SIV strains from which Nef proteins were included in this study are shown on the left.