5OYM

HIV Integrase Binding Domain of Lens Epithelium-Derived Growth Factor

Summary for 5OYM

• Entry DOI: 10.2210/pdb5oym/pdb
• Descriptor: PC4 and SFRS1-interacting protein (2 entities in total)
• Functional Keywords: integrase binding, transciptional co-activator, domain swap, transcription
• Biological source: Homo sapiens (Human)
• Cellular location: Nucleus : O75475
• Total number of polymer chains: 8
• Total formula weight: 95181.53

Authors

Rabbitts, T.H.,Phillips, S.E.V.,Cruz-Migoni, A.,Carr, S.B.,Hannon, C. (deposition date: 2017-09-11, release date: 2018-03-07, Last modification date: 2024-01-17)

Primary citation

Hannon, C.,Cruz-Migoni, A.,Platonova, O.,Owen, R.L.,Nettleship, J.E.,Miller, A.,Carr, S.B.,Harris, G.,Rabbitts, T.H.,Phillips, S.E.V.
Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor.
Acta Crystallogr F Struct Biol Commun, 74:143-149, 2018

PubMed 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 P2, 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.

PubMed: 29497017
DOI: 10.1107/S2053230X18001553

Experimental method

X-RAY DIFFRACTION (2.05 Å)