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• W2016888788 abstract "One of many protein-protein interactions modulated upon DNA damage is that of the single-stranded DNA-binding protein, replication protein A (RPA), with the p53 tumor suppressor. Here we report the crystal structure of RPA residues 1-120 (RPA70N) bound to the N-terminal transactivation domain of p53 (residues 37-57; p53N) and, by using NMR spectroscopy, characterize two mechanisms by which the RPA/p53 interaction can be modulated. RPA70N forms an oligonucleotide/oligosaccharide-binding fold, similar to that previously observed for the ssDNA-binding domains of RPA. In contrast, the N-terminal p53 transactivation domain is largely disordered in solution, but residues 37-57 fold into two amphipathic helices, H1 and H2, upon binding with RPA70N. The H2 helix of p53 structurally mimics the binding of ssDNA to the oligonucleotide/oligosaccharide-binding fold. NMR experiments confirmed that both ssDNA and an acidic peptide mimicking a phosphorylated form of RPA32N can independently compete the acidic p53N out of the binding site. Taken together, our data suggest a mechanism for DNA damage signaling that can explain a threshold response to DNA damage." @default.
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• W2016888788 date "2005-10-17" @default.
• W2016888788 modified "2023-10-18" @default.
• W2016888788 title "Single-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein A" @default.
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• W2016888788 doi "https://doi.org/10.1073/pnas.0504614102" @default.
• W2016888788 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1266094" @default.
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