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.
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| http://dx.doi.org/10.1016/j.dib.2020.106680 | DOI Listing |
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Nuclear magnetic resonance spectral data of the USP7 TRAF and UBL1-2 domains in complex with DNA polymerase ι peptides.
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Department of Molecular Biology and Biophysics, UConn Health, Farmington, CT 06030, USA.
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.
View Article and Find Full Text PDFDNA Polymerase ι Interacts with Both the TRAF-like and UBL1-2 Domains of USP7.
J Mol Biol
January 2021
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. Electronic address:
Reversible protein ubiquitination is an essential signaling mechanism within eukaryotes. Deubiquitinating enzymes are critical to this process, as they mediate removal of ubiquitin from substrate proteins. Ubiquitin-specific protease 7 (USP7) is a prominent deubiquitinating enzyme, with an extensive network of interacting partners and established roles in cell cycle activation, immune responses and DNA replication.
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Article Synopsis
- Human USP7 is a crucial enzyme that prevents protein degradation and plays a key role in regulating the stability of transcription factors and tumor suppressors, influencing cancer development, particularly in prostate and lung cancers.
- The study identified the structure of the UBL1 domain of USP7 and explored its interaction with the herpesvirus protein ICP0, which is vital for the virus's ability to infect cells and reactivate.
- The research findings suggest that targeting USP7 could lead to new antiviral and anticancer treatments by enhancing our understanding of its substrate interactions.
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