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Cloning, purification and structure determination of the HIV integrase‐binding domain of lens epithelium‐derived growth factor
Author(s) -
Han Clare,
Cruz-Migoni Abimael,
Platonova Olga,
Owen Robin L.,
Nettleship Joanne E.,
Miller Ami,
Carr Stephen B.,
Harris Gemma,
Rabbitts Terence H.,
Phillips Simon E. V.
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18001553
Subject(s) - integrase , histone octamer , chemistry , cloning (programming) , escherichia coli , monomer , crystallography , recombinant dna , biology , microbiology and biotechnology , biochemistry , dna , gene , organic chemistry , nucleosome , histone , polymer , computer science , programming language
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 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.