ArticleNucleic acids research2011
Quaternary structure of the specific p53-DNA complex reveals the mechanism of p53 mutant dominance.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Correlation of p53 oligomeric status and its subcellular localization in the presence of the AML-associated NPM mutant.PloS one · 2025Article
- Structural assessment of the full-length wild-type tumor suppressor protein p53 by mass spectrometry-guided computational modeling.Scientific reports · 2023Article
- Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR.Biochemistry · 2022Article
- The Δ40p53 isoform inhibits p53-dependent eRNA transcription and enables regulation by signal-specific transcription factors during p53 activation.PLoS biology · 2021Article
- Structural and Drug Targeting Insights on Mutant p53.Cancers · 2021Review
- Mesoscopic protein-rich clusters host the nucleation of mutant p53 amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Single molecule studies reveal that p53 tetramers dynamically bind response elements containing one or two half sites.Scientific reports · 2020Article
- Mdm2: Open questions.Cancer science · 2020Review
- How p53 Molecules Solve the Target DNA Search Problem: A Review.International journal of molecular sciences · 2020Review
- Wild-type p53 oligomerizes more efficiently than p53 hot-spot mutants and overcomes mutant p53 gain-of-function via a "dominant-positive" mechanism.Oncotarget · 2018Article
- Article
- A novel TP53 germline inframe deletion identified in a Spanish series of Li-fraumeni syndrome suspected families.Familial cancer · 2017Article
- Germline TP53 mutations result into a constitutive defect of p53 DNA binding and transcriptional response to DNA damage.Human molecular genetics · 2017Article
- Design of a molecular support for cryo-EM structure determination.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Two p53 tetramers bind one consensus DNA response element.Nucleic acids research · 2016Article
- APR-246 overcomes resistance to cisplatin and doxorubicin in ovarian cancer cells.Cell death & disease · 2015Article
- A dominant-negative mutation of mouse Lmx1b causes glaucoma and is semi-lethal via LDB1-mediated dimerization [corrected].PLoS genetics · 2014Article
- Structures of oncogenic, suppressor and rescued p53 core-domain variants: mechanisms of mutant p53 rescue.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Molecular dynamics of the full-length p53 monomer.Cell cycle (Georgetown, Tex.) · 2013Article
- Expanding the prion concept to cancer biology: dominant-negative effect of aggregates of mutant p53 tumour suppressor.Bioscience reports · 2013Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
The p53 tumour suppressor is a transcriptional activator that controls cell fate in response to various stresses. p53 can initiate cell cycle arrest, senescence and/or apoptosis via transactivation of p53 target genes, thus preventing cancer onset. Mutations that impair p53 usually occur in the core domain and negate the p53 sequence-specific DNA binding. Moreover, these mutations exhibit a dominant negative effect on the remaining wild-type p53. Here, we report the cryo electron microscopy structure of the full-length p53 tetramer bound to a DNA-encoding transcription factor response element (RE) at a resolution of 21 A. While two core domains from both dimers of the p53 tetramer interact with DNA within the complex, the other two core domains remain available for binding another DNA site. This finding helps to explain the dominant negative effect of p53 mutants based on the fact that p53 dimers are formed co-translationally before the whole tetramer assembles; therefore, a single mutant dimer would prevent the p53 tetramer from binding DNA. The structure indicates that the Achilles' heel of p53 is in its dimer-of-dimers organization, thus the tetramer activity can be negated by mutation in only one allele followed by tumourigenesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.