Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA
Abstract
The solution structure of the central domain of the human nucleotide excision repair protein XPA, which binds to damaged DNA and replication protein A (RPA), was determined by nuclear magnetic resonance (NMR) spectroscopy. The central domain consists of a zinc-containing subdomain and a C-terminal subdomain. The zinc-containing subdomain has a compact globular structure and is distinct from the zinc-fingers found in transcription factors. The C-terminal subdomain folds into a novel alpha/beta structure with a positively charged superficial cleft. From the NMR spectra of the complexes, DNA and RPA binding surfaces are suggested.
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Hilton et al. showed that XPA uses a larger DNA-binding domain for ds-ssDNA junctions than was previously described for repair substrates.
“Hilton et al. recently demonstrated that in binding to ds-ssDNA junctions XPA employs a larger DNA-binding domain 102 than was previously described for repair substrates 103, 104.”
From Xeroderma Pigmentosa Group A (XPA), Nucleotide Excision Repair and Regulation by ATR in Response to Ultraviolet Irradiation (2017) · cites this paper as [104]
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- Authors
- Ikegami, T., Kuraoka, I., Saijo, M., Kodo, N., Kyogoku, Y., Morikawa, K., Tanaka, K., & Shirakawa, M.
- Affiliations
- Nara Institute of Science and Technology (JP)
- The University of Osaka (JP)
- Institute for Protein Research, The University of Osaka (JP)
- Biomolecular Engineering Research Institute (Japan) (JP)
- Corresponding author
- Shirakawa, Masahiro
- Venue
- Nature Structural & Molecular Biology
- Published
- 1998-08
- Volume
- 5
- Issue
- 8
- Pages
- 701-706
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- DOI
- 10.1038/1400
- OpenAlex
- W2020761966
- Cited by
- 139
- References
- 27
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 3 · 2023: 4 · 2022: 3 · 2021: 2 · 2020: 4 · 2019: 8 · 2018: 5 · 2017: 8 · 2016: 7 · 2015: 4 · 2014: 9 · 2013: 2 · 2012: 2
- FWCI
- 2.44
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- XPA, nucleotide excision repair, DNA repair, replication protein A, DNA binding, alpha/beta fold, protein structure, solution structure, protein-DNA complex
- MeSH terms
- Amino Acid Sequence, Binding Sites, DNA Repair, DNA-Binding Proteins, Humans, Metalloproteins, Models, Molecular, Molecular Sequence Data, Protein Conformation, Xeroderma Pigmentosum, Zinc, RNA-Binding Proteins, Sequence Homology, Amino Acid, Nuclear Magnetic Resonance, Biomolecular, Replication Protein A, Xeroderma Pigmentosum Group A Protein
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