Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor.
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ICR Authors
Authors
Hannon, C
Cruz-Migoni, A
Platonova, O
Owen, RL
Nettleship, JE
Miller, A
Carr, SB
Harris, G
Rabbitts, TH
Phillips, SEV
Cruz-Migoni, A
Platonova, O
Owen, RL
Nettleship, JE
Miller, A
Carr, SB
Harris, G
Rabbitts, TH
Phillips, SEV
Document Type
Journal Article
Date
2018-03-01
Date Accepted
2018-01-23
Abstract
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.
Citation
Acta crystallographica. Section F, Structural biology communications, 2018, 74 (Pt 3), pp. 143 - 149
Source Title
Publisher
INT UNION CRYSTALLOGRAPHY
ISSN
2053-230X
eISSN
2053-230X
Collections
Research Team
Chromosomal Translocations and Intracellular Antibody Therapeutics