|
Figure 7.
Figure 7. Helical wheel representation of the helix 53-
78 in (52-96)Vpr illustrating the leucine zipper-like
monodimeric interaction. The scheme displays residues
53 to 81. The hydrophobic residues are found in pos-
itions d, a, g and e, showing the amphiphilic nature of
the helix. A second identical (52-96)Vpr helix (grey)
could contact the first one with the hydrophobic resi-
dues in a and d positions in a homodimer.
|