Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor.
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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 P2 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.
Adaptor Proteins, Signal Transducing
Amino Acid Sequence
Chromosomal Translocations and Intracellular Antibody Therapeutics
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Acta crystallographica. Section F, Structural biology communications, 2018, 74 (Pt 3), pp. 143 - 149