dc.contributor.author | Hannon, C | |
dc.contributor.author | Cruz-Migoni, A | |
dc.contributor.author | Platonova, O | |
dc.contributor.author | Owen, RL | |
dc.contributor.author | Nettleship, JE | |
dc.contributor.author | Miller, A | |
dc.contributor.author | Carr, SB | |
dc.contributor.author | Harris, G | |
dc.contributor.author | Rabbitts, TH | |
dc.contributor.author | Phillips, SEV | |
dc.date.accessioned | 2020-12-21T14:05:20Z | |
dc.date.issued | 2018-03-01 | |
dc.identifier.citation | Acta crystallographica. Section F, Structural biology communications, 2018, 74 (Pt 3), pp. 143 - 149 | |
dc.identifier.issn | 2053-230X | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/4261 | |
dc.identifier.eissn | 2053-230X | |
dc.identifier.doi | 10.1107/s2053230x18001553 | |
dc.description.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. | |
dc.format | Print-Electronic | |
dc.format.extent | 143 - 149 | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | INT UNION CRYSTALLOGRAPHY | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0 | |
dc.subject | Humans | |
dc.subject | HIV Integrase | |
dc.subject | Adaptor Proteins, Signal Transducing | |
dc.subject | Transcription Factors | |
dc.subject | Crystallization | |
dc.subject | Crystallography, X-Ray | |
dc.subject | Amino Acid Sequence | |
dc.subject | Catalytic Domain | |
dc.subject | Protein Conformation | |
dc.subject | Models, Molecular | |
dc.title | Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor. | |
dc.type | Journal Article | |
dcterms.dateAccepted | 2018-01-23 | |
rioxxterms.versionofrecord | 10.1107/s2053230x18001553 | |
rioxxterms.licenseref.uri | https://creativecommons.org/licenses/by/4.0 | |
rioxxterms.licenseref.startdate | 2018-03 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | Acta crystallographica. Section F, Structural biology communications | |
pubs.issue | Pt 3 | |
pubs.notes | Not known | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR/Primary Group | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Therapeutics | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Therapeutics/Chromosomal Translocations and Intracellular Antibody Therapeutics | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR/Primary Group | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Therapeutics | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Therapeutics/Chromosomal Translocations and Intracellular Antibody Therapeutics | |
pubs.publication-status | Published | |
pubs.volume | 74 | |
pubs.embargo.terms | Not known | |
icr.researchteam | Chromosomal Translocations and Intracellular Antibody Therapeutics | |
dc.contributor.icrauthor | Rabbitts, Terence | |