Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor
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 crystall...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal article |
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International Union of Crystallography
2018
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| _version_ | 1797053911335436288 |
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| author | Hannon, C Cruz-Migoni, A Platonova, O Owen, R Nettleship, J Miller, A Carr, S Harris, G Rabbitts, T Phillips, S |
| author_facet | Hannon, C Cruz-Migoni, A Platonova, O Owen, R Nettleship, J Miller, A Carr, S Harris, G Rabbitts, T Phillips, S |
| author_sort | Hannon, C |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T18:50:12Z |
| format | Journal article |
| id | oxford-uuid:0ff72385-6801-4db4-90b4-547106196781 |
| institution | University of Oxford |
| last_indexed | 2024-03-06T18:50:12Z |
| publishDate | 2018 |
| publisher | International Union of Crystallography |
| record_format | dspace |
| spelling | oxford-uuid:0ff72385-6801-4db4-90b4-5471061967812022-03-26T09:53:55ZCloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factorJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:0ff72385-6801-4db4-90b4-547106196781Symplectic Elements at OxfordInternational Union of Crystallography2018Hannon, CCruz-Migoni, APlatonova, OOwen, RNettleship, JMiller, ACarr, SHarris, GRabbitts, TPhillips, SLens 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. |
| spellingShingle | Hannon, C Cruz-Migoni, A Platonova, O Owen, R Nettleship, J Miller, A Carr, S Harris, G Rabbitts, T Phillips, S Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor |
| title | Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor |
| title_full | Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor |
| title_fullStr | Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor |
| title_full_unstemmed | Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor |
| title_short | Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor |
| title_sort | cloning purification and structure determination of the hiv integrase binding domain of lens epithelium derived growth factor |
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