The DNA-binding domain of HIV-1 integrase has an SH3-like fold.

Article Details

Citation

Eijkelenboom AP, Lutzke RA, Boelens R, Plasterk RH, Kaptein R, Hard K

The DNA-binding domain of HIV-1 integrase has an SH3-like fold.

Nat Struct Biol. 1995 Sep;2(9):807-10.

PubMed ID
7552753 [ View in PubMed
]
Abstract

We have determined the solution structure of the DNA-binding domain of HIV-1 integrase by nuclear magnetic resonance spectroscopy. In solution, this carboxyterminal region of integrase forms a homodimer, consisting of two structures that closely resemble Src-homology 3 (SH3) domains. Lys 264, previously identified by mutagenesis studies to be important for DNA binding of the integrase, as well as several adjacent basic amino acids are solvent exposed. The identification of an SH3-like domain in integrase provides a new potential target for drug design.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Gag-Pol polyproteinP03366Details