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1H, 15N, 13C resonance assignments for proteasome shuttle factor hHR23a

  1. Author:
    Chen,Xiang [ORCID]
    Walters,Kylie [ORCID]

  2. Author Address

    Protein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, 21702, USA., Protein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, 21702, USA. kylie.walters@nih.gov.,
    1. Year: 2023
    2. Date: Oct 09
    3. Epub Date: 2023 10 09
  2. Journal: Biomolecular NMR Assignments
  4. Type of Article: Article
  1. Abstract:

    hHR23a (human homolog of Rad23 a) functions in nucleotide excision repair and proteasome-mediated protein degradation. It contains an N-terminal ubiquitin-like (UBL) domain, an xeroderma pigmentosum C (XPC)-binding domain, and a ubiquitin-associated (UBA) domain preceding and following the XPC-binding domain. Each of the four structural domains are connected by flexible linker regions. We report in this NMR study, the 1H, 15N and 13C resonance assignments for the backbone and sidechain atoms of the hHR23a full-length protein with BioMagResBank accession number 52059. Assignments are 97% and 87% for the backbone (NH, N, C', Ca, and Ha) and sidechain atoms of the hHR23a structured regions. The secondary structural elements predicted from the NMR data fit well to the hHR23a NMR structure. The assignments described in this manuscript can be used to apply NMR for studies of hHR23a with its binding partners. © 2023. This is a U.S. Government work and not under copyright protection in the US; foreign copyright protection may apply.

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External Sources

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  2. DOI: 10.1007/s12104-023-10157-z
  3. PMID: 37812322
  4. PII : 10.1007/s12104-023-10157-z

Library Notes

  1. Fiscal Year: FY2023-2024
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