دورية أكاديمية
Nuclear magnetic resonance spectral data of the USP7 TRAF and UBL1-2 domains in complex with DNA polymerase ι peptides.
| العنوان: | Nuclear magnetic resonance spectral data of the USP7 TRAF and UBL1-2 domains in complex with DNA polymerase ι peptides. |
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| المؤلفون: | Valles GJ; Department of Molecular Biology and Biophysics, UConn Health, Farmington, CT 06030, USA., Ashton NW; Laboratory of Genomic Integrity, National Institute of Child Health and Human Development, National Institutes of Health, 9800 Medical Center Drive, Bethesda, MD 20892-3371, USA., Jaiswal N; Department of Molecular Biology and Biophysics, UConn Health, Farmington, CT 06030, USA., Woodgate R; Laboratory of Genomic Integrity, National Institute of Child Health and Human Development, National Institutes of Health, 9800 Medical Center Drive, Bethesda, MD 20892-3371, USA., Bezsonova I; Department of Molecular Biology and Biophysics, UConn Health, Farmington, CT 06030, USA. |
| المصدر: | Data in brief [Data Brief] 2020 Dec 23; Vol. 34, pp. 106680. Date of Electronic Publication: 2020 Dec 23 (Print Publication: 2021). |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier B.V Country of Publication: Netherlands NLM ID: 101654995 Publication Model: eCollection Cited Medium: Internet ISSN: 2352-3409 (Electronic) Linking ISSN: 23523409 NLM ISO Abbreviation: Data Brief Subsets: PubMed not MEDLINE |
| أسماء مطبوعة: | Original Publication: [Amsterdam] : Elsevier B.V., [2014]- |
| مستخلص: | This data article is related to the publication 'DNA polymerase ι interacts with both the TRAF-like and UBL1-2 domains of USP7' [1]. Ubiquitin-specific protease 7 (USP7) is an essential deubiquitinating enzyme with characterized substrates in many cellular pathways. Established USP7 substrates interact with one of two major binding sites, located on the N-terminal TRAF-like (TRAF) domain and the first and second UBL domains (UBL1-2) within the C-terminal tail. In this article, we present complete nuclear magnetic resonance (NMR) spectroscopy data used to characterize direct interactions between USP7 and its novel substrate DNA polymerase iota (Pol ι), that binds both TRAF and UBL1-2 domains. The detailed description of the NMR data, and the methodology used for processing and analysis, will add to the reproducibility and transparency of the companion research article, as well as aid in the reuse of these data. Competing Interests: The authors declare that they have no known competing financial interests or personal relationships which have or could be perceived to have influenced the work reported in this article. |
| References: | J Biol Chem. 2015 Sep 18;290(38):22907-18. (PMID: 26224631) Biophys J. 2017 Apr 25;112(8):1529-1534. (PMID: 28445744) J Mol Biol. 2021 Jan 22;433(2):166733. (PMID: 33279577) J Biomol NMR. 1995 Nov;6(3):277-93. (PMID: 8520220) |
| معلومات مُعتمدة: | P41 GM111135 United States GM NIGMS NIH HHS; R01 GM123249 United States GM NIGMS NIH HHS; R35 GM128864 United States GM NIGMS NIH HHS |
| فهرسة مساهمة: | Keywords: DNA polymerase iota; Deubiquitination; Herpesvirus-associated ubiquitin-specific protease; Translesion synthesis; Ubiquitin-like domain; Ubiquitin-specific protease 7 |
| تواريخ الأحداث: | Date Created: 20210113 Latest Revision: 20210115 |
| رمز التحديث: | 20240628 |
| مُعرف محوري في PubMed: | PMC7788100 |
| DOI: | 10.1016/j.dib.2020.106680 |
| PMID: | 33437851 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 2352-3409 |
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| DOI: | 10.1016/j.dib.2020.106680 |