Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor
At a Glance
Section titled āAt a Glanceā| Metadata | Details |
|---|---|
| Publication Date | 2018-02-26 |
| Journal | Acta Crystallographica Section F Structural Biology Communications |
| Authors | Clare Hannon, Abimael Cruz-Migoni, Olga Platonova, Robin L. Owen, Joanne E. Nettleship |
| Institutions | Diamond Light Source, John Radcliffe Hospital |
| Citations | 5 |
Abstract
Section titled āAbstractāLens 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 Escherichia coli , purified and crystallized by sitting-drop vapour diffusion. X-ray diffraction data were collected at Diamond Light Source to a resolution of 2.05 Ć . The crystals belonged to space group P 2 1 , 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.