Residue | Hck SH3 | PAK2 | MHCI | EVI | CD4 |
|---|
EEEE/AAAA
| # | +1 | −1 | +1 | ++1 |
V66A
| # | + | ++ | + | ++ |
G67A
| # | − | − | − | ++ |
F68A
| # | − | − | − | + |
P69A
| ++3 | −3,5 | ++6 | −5 | ++6 |
P72G
| − | − | + | − | ++ |
Q73R
| ++ | − | ++ | + | ++ |
V74I
| − | ++ | ++ | ++ | ++ |
P75G
| − | − | + | + | ++ |
L76V
| ++ | + | + | + | ++ |
R77K
| − | − | ++ | − | ++ |
P78G
| ++ | + | − | ++ | ++ |
F90A
| ++ | − | + | + | ++ |
D123E
| # | ++2,4 | −2,4 | −4 | −2,4 |
- Results are presented from this report unless otherwise indicated. 1Baugh et al. [29]; 2Kwak et al. [31]; 3Manninen et al. [20]; 4O’Neil et al. [32]; 5Wiskerchen et al. [41]; 6Yamada et al. [33]. Hck SH3, in vitro binding of Nef to Hck SH3 domain; PAK2, Nef/activated PAK2 complex formation; MHCI, MHCI downregulation; EVI, enhancement of virion infectivity; CD4, CD4 downregulation. #, indicates that the residue is outside of the known Nef-Hck SH3 interface [23, 24]; “++” activity of mutated protein is >75% of wild type protein; “+” activity is between 25% and 75% of wild type; “-“ activity is less that 25% of wild type. EEEE/AAAA is the quadruple mutation of the tetra-glutamate segment (amino acids 62–65) of Nef mutated to four alanines.
