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• W2967887538 endingPage "17479" @default.
• W2967887538 startingPage "17470" @default.
• W2967887538 abstract "The most frequently mutated protein in human cancer is p53, a transcription factor (TF) that regulates myriad genes instrumental in diverse cellular outcomes including growth arrest and cell death. Cell context-dependent p53 modulation is critical for this life-or-death balance, yet remains incompletely understood. Here we identify sequence signatures enriched in genomic p53-binding sites modulated by the transcription cofactor iASPP. Moreover, our p53-iASPP crystal structure reveals that iASPP displaces the p53 L1 loop-which mediates sequence-specific interactions with the signature-corresponding base-without perturbing other DNA-recognizing modules of the p53 DNA-binding domain. A TF commonly uses multiple structural modules to recognize its cognate DNA, and thus this mechanism of a cofactor fine-tuning TF-DNA interactions through targeting a particular module is likely widespread. Previously, all tumor suppressors and oncoproteins that associate with the p53 DNA-binding domain-except the oncogenic E6 from human papillomaviruses (HPVs)-structurally cluster at the DNA-binding site of p53, complicating drug design. By contrast, iASPP inhibits p53 through a distinct surface overlapping the E6 footprint, opening prospects for p53-targeting precision medicine to improve cancer therapy." @default.
• W2967887538 created "2019-08-22" @default.
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• W2967887538 date "2019-08-08" @default.
• W2967887538 modified "2023-10-15" @default.
• W2967887538 title "iASPP mediates p53 selectivity through a modular mechanism fine-tuning DNA recognition" @default.
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• W2967887538 doi "https://doi.org/10.1073/pnas.1909393116" @default.
• W2967887538 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6717262" @default.
• W2967887538 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31395738" @default.

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