Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor
Hannon C., Cruz-Migoni A., Platonova O., Owen RL., Nettleship JE., Miller A., Carr SB., Harris G., Rabbitts TH., Phillips SEV.
<jats:p>Lens epithelium-derived growth factor (LEDGF)/p75 is the dominant binding partner of HIV-1 integrase in human cells. The crystal structure of the HIV integrase-binding domain (IBD) of LEDGF has been determined in the absence of ligand. IBD was overexpressed in<jats:italic>Escherichia coli</jats:italic>, purified and crystallized by sitting-drop vapour diffusion. X-ray diffraction data were collected at Diamond Light Source to a resolution of 2.05 Å. The crystals belonged to space group<jats:italic>P</jats:italic>2<jats:sub>1</jats:sub>, with eight polypeptide chains in the asymmetric unit arranged as an unusual octamer composed of four domain-swapped IBD dimers. IBD exists as a mixture of monomers and dimers in concentrated solutions, but the dimers are unlikely to be biologically relevant.</jats:p>