دورية أكاديمية

Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor.

التفاصيل البيبلوغرافية
العنوان: Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor.
المؤلفون: Hannon, C, Cruz-Migoni, A, Platonova, O, Owen, RL, Nettleship, JE, Miller, A, Carr, SB, Harris, G, Rabbitts, TH, Phillips, SEV
المساهمون: Rabbitts, Terence
بيانات النشر: INT UNION CRYSTALLOGRAPHY
سنة النشر: 2020
المجموعة: The Institute of Cancer Research (ICR): Publications Repository
مصطلحات موضوعية: Humans, HIV Integrase, Adaptor Proteins, Signal Transducing, Transcription Factors, Crystallization, Crystallography, X-Ray, Amino Acid Sequence, Catalytic Domain, Protein Conformation, Models, Molecular
الوصف: 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.
نوع الوثيقة: article in journal/newspaper
وصف الملف: Print-Electronic; 149; application/pdf
اللغة: English
تدمد: 2053-230X
العلاقة: Acta crystallographica. Section F, Structural biology communications, 2018, 74 (Pt 3), pp. 143 - 149; https://repository.icr.ac.uk/handle/internal/4261Test
DOI: 10.1107/s2053230x18001553
الإتاحة: https://doi.org/10.1107/s2053230x18001553Test
https://repository.icr.ac.uk/handle/internal/4261Test
حقوق: https://creativecommons.org/licenses/by/4.0Test
رقم الانضمام: edsbas.A143EA24
قاعدة البيانات: BASE
الوصف
تدمد:2053230X
DOI:10.1107/s2053230x18001553