Fig. 6

Comparison of N-terminal oligomerization domains of primate lentivirus Revs. a Sequence logo of HIV-1 and HIV-2 Rev, depicting coiled-coil (C-C) registers predicted for HIV-2 and the corresponding region in HIV-1 Rev sequences predicted not to contain coiled-coils (no C-C). Shaded outlines indicate ‘a’ and ‘d’ core registers, underlined residues indicate major genetic differences between HIV-1 and HIV-2. Colored residues indicate polar residues and black residues indicate hydrophobic residues; red and blue colored residues represent polar charged residues, and green colored residues represent polar non-charged residues. b Sequence logo depicting coiled-coil registers predicted for a subset of SIV Rev sequences predicted to contain coiled-coils and the corresponding region in SIV Rev sequences predicted not to contain coiled-coils. Shaded outlines indicate ‘a’ and ‘d’ core registers and underlined residues indicate sites of genetic differences. Colored residues indicate polar residues and black residues indicate hydrophobic residues; red and blue colored residues represent polar charged residues, and green colored residues represent polar non-charged residues. c Helical wheel diagrams of the coiled-coil region of HIV-2 Rev and the corresponding region in HIV-1 Rev. Filled circles indicate hydrophobic residues and dashed lines indicate predicted interaction interfaces, designated A-interface or B-interface. Numbered residues on the helical wheel of HIV-1 indicate residues known to mediate dimerization and oligomerization in published HIV-1 crystal structures [29, 37]. d Helical wheel diagrams of the coiled-coil region for the subset of SIV Revs predicted to contain coiled-coils, and the corresponding region in SIV Revs predicted not to contain coiled-coils. Filled circles indicate hydrophobic residues and dashed lines indicate two predicted interaction interfaces, designated A-interface or B-interface