ArticleNucleic acids research2001
DNA-XPA interactions: a (31)P NMR and molecular modeling study of dCCAATAACC association with the minimal DNA-binding domain (M98-F219) of the nucleotide excision repair protein XPA.
Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 29 citations in OpenAlex.
- The XPA Protein-Life under Precise Control.Cells · 2022Review
- Characterizing the Binding Interactions between DNA-Binding Proteins, XPA and XPE: A Molecular Dynamics Approach.ACS omega · 2018Article
- Design and Structure-Guided Development of Novel Inhibitors of the Xeroderma Pigmentosum Group A (XPA) Protein-DNA Interaction.Journal of medicinal chemistry · 2017Article
- XPA: A key scaffold for human nucleotide excision repair.DNA repair · 2016Review
- Role of the XPA protein in the NER pathway: A perspective on the function of structural disorder in macromolecular assembly.Computational and structural biotechnology journal · 2016Review
- A new structural insight into XPA-DNA interactions.Bioscience reports · 2014Article
- Protein modification by adenine propenal.Chemical research in toxicology · 2014Article
- Redefining the DNA-binding domain of human XPA.Journal of the American Chemical Society · 2014Article
- Functional binding of hexanucleotides to 3C protease of hepatitis A virus.Nucleic acids research · 2012Article
- Identification of novel small molecule inhibitors of the XPA protein using in silico based screening.ACS chemical biology · 2010Article
- Checkpoint kinase ATR promotes nucleotide excision repair of UV-induced DNA damage via physical interaction with xeroderma pigmentosum group A.The Journal of biological chemistry · 2009Article
- Characterization of protein secondary structure from NMR chemical shifts.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- Article
- Chemical shift changes provide evidence for overlapping single-stranded DNA- and XPA-binding sites on the 70 kDa subunit of human replication protein A.Nucleic acids research · 2003Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Recent NMR-based, chemical shift mapping experiments with the minimal DNA-binding domain of XPA (XPA-MBD: M98-F219) suggest that a basic cleft located in the loop-rich subdomain plays a role in DNA-binding. Here, XPA-DNA interactions are further characterized by NMR spectroscopy from the vantage point of the DNA using a single-stranded DNA nonamer, dCCAATAACC (d9). Up to 2.5 molar equivalents of XPA-MBD was titrated into a solution of d9. A subset of (31)P resonances of d9 were observed to broaden and/or shift providing direct evidence that XPA-MBD binds d9 by a mechanism that perturbs the phosphodiester backbone of d9. The interior five residues of d9 broadened and/or shifted before (31)P resonances of phosphate groups at the termini, suggesting that when d9 is bound to XPA-MBD the internal residues assume a correlation time that is characteristic of the molecular weight of the complex while the residues at the termini undergo a fraying motion away from the surface of the protein on a timescale such that the line widths are more characteristic of the molecular weight of ssDNA. A molecular model of the XPA-MBD complex with d9 was calculated based on the (15)N (XPA-MBD) and (31)P (d9) chemical shift mapping studies and on the assumption that electrostatic interactions drive the complex formation. The model shows that a nine residue DNA oligomer fully covers the DNA-binding surface of XPA and that there may be an energetic advantage to binding DNA in the 3'-->5' direction rather than in the 5'-->3' direction (relative to XPA-MBD alpha-helix-3).
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