A Symmetric Region of the HIV-1 Integrase Dimerization Interface Is Essential for Viral Replication
Figure 1
A symmetric region of the HIV-1 dimerization interface is conserved across other lentiviruses.
(A) PyMOL representation of the highly symmetric region at the HIV-1 IN dimeric interface. A four-tiered aromatic interaction between W61 and W108 from each IN monomer is flanked by two salt bridges composed of E85 and R107, and E87 and K103 from each monomer. The four-tiered aromatic interaction donates at least −10 kcal/mol of stabilization energy to the interface. (B) Sequence alignment of relevant lentiviral IN residues, beginning at IN residue 55. Red text denotes highly conserved residues, while blue signifies moderately conserved. W61, E85, E87, K103, R107, and W108 are all completely conserved throughout HIV-1, SHIV, SIV, and HIV-1 viruses. Aromaticity is heavily conserved across most lentiviruses for positions 61 and 108.