Multimerization of HIV-1 integrase hinges on conserved SH3-docking platforms

Meytal Galilee; Akram Alian

Whereas the peptide mainly represented the CDR3sequence and was expected to also represent CDR3 binding pattern (to dock at the CCD/NTD interface between α4 and the finger loop, (Figure 1C )), the peptide surprisingly docked underneath α4 to mostly resemble the binding of CDR2 at site-1 ( Figure 2A ). Superimposing the CCD-peptide structure onto that of the HIV-1 intasome reveals potential steric interference with the CCD docking platform of CTD but not NTD at site-1 ( Figure 2E , top). Similarly, the symmetry related molecule of the peptide bound at site-2 reveals potential interference with the docking of another CTD ( Figure 2E , bottom).