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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 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 Å. The crystals belonged to space group P21, 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.

Original publication

DOI

10.1107/S2053230X18001553

Type

Journal article

Journal

Acta crystallogr f struct biol commun

Publication Date

01/03/2018

Volume

74

Pages

143 - 149

Keywords

HIV integrase-binding domain, domain swapping, human immunodeficiency virus, lens epithelium-derived growth factor