THE DNA-BINDING DOMAIN OF HIV-1 INTEGRASE HAS AN SH3-LIKE FOLD

We have determined the solution structure of the DNA-binding domain of HIV-1 integrase by nuclear magnetic resonance spectroscopy. In soluti on, this carboxy-terminal region of integrase forms a homodimer, consi sting of two structures that closely resemble Src-homology 3 (SH3) dom ains. Lys 264 previously identified by mutagenesis studies to be impor tant for DNA binding of the integrase, as well as several adjacent bas ic amino acids are solvent exposed, The identification of an SH3-like domain in integrase provides a new potential target for drug design.