The C-terminal domain of human immunodeficiency virus type 1 (HIV-1) integrase (IN) is a
dimer that binds to DNA in a nonspecific manner. The structure of the minimal region …

HIV-1 integrase (IN) mediates the insertion of viral cDNA into the cell genome, a vital
process for replication. This step is catalyzed by two separate DNA reaction events, termed …

Abstract HIV-1 integrase (IN) oligomerization and DNA recognition are crucial steps for the
subsequent events of the integration reaction. Recent advances described the involvement …

HIV-1 integration into the host cell genome is a multistep process catalyzed by the virally-
encoded integrase (IN) protein. In view of the difficulty of obtaining a stable DNA-bound IN at …

HIV-1 integrase specifically recognizes and cleaves viral end DNA during the initial step of
retroviral integration. The protein and DNA determinants of the specificity of viral end DNA …

HIV-1 integrase (IN) is an important target for contemporary antiretroviral drug design
research. Historically, efforts at inactivating the enzyme have focused upon blocking its …

To gain insight into the importance of conserved residues in the core domain of HIV-1 IN, we
performed site-directed mutagenesis of the full-length enzyme, overexpressed the mutant …

Results of in vitro assays identified residues in the C-terminal domain (CTD) of human
immunodeficiency virus type 1 (HIV-1) integrase (IN) important for IN-IN and IN-DNA …

Genetic robustness (tolerance of mutation) may be a naturally selected property in some
viruses, because it should enhance adaptability. Robustness should be especially beneficial …

The 3′-processing of the extremities of viral DNA is the first of two reactions catalyzed by
HIV-1 integrase (IN). High order IN multimers (tetramers) are required for complete …