ArticleJournal of biosciences2007
Mechanism of DNA-binding loss upon single-point mutation in p53.
Article in Journal of biosciences, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Integrated molecular dynamics elucidation of TP53 H179 zinc-binding variants: genomic and structural characterization across NSCLC subtypes.Frontiers in bioinformatics · 2026Article
- NUAK2 and RCan2 participate in the p53 mutant pro-tumorigenic network.Biology direct · 2021Article
- Significance of avian linker histone (H1) polymorphic variation.Journal of biosciences · 2018Review
- Therapeutic potential of Bcl-xOncology letters · 2018Article
- Article
- Cancer therapeutic approach based on conformational stabilization of mutant p53 protein by small peptides.Oncotarget · 2016Article
- A High-Throughput Cell-Based Screen Identified a 2-[(E)-2-Phenylvinyl]-8-Quinolinol Core Structure That Activates p53.PloS one · 2016Article
- Novel role of PELP1 in regulating chemotherapy response in mutant p53-expressing triple negative breast cancer cells.Breast cancer research and treatment · 2015Article
- Investigating DNA Binding and Conformational Variation in Temperature Sensitive p53 Cancer Mutants Using QM-MM Simulations.PloS one · 2015Article
- QM-MM simulations on p53-DNA complex: a study of hot spot and rescue mutants.Journal of molecular modeling · 2013Article
- Prediction of DNA-binding specificity in zinc finger proteins.Journal of biosciences · 2012Article
- Analyzing effects of naturally occurring missense mutations.Computational and mathematical methods in medicine · 2012Article
- Effects of temperature on the p53-DNA binding interactions and their dynamical behavior: comparing the wild type to the R248Q mutant.PloS one · 2011Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Over 50% of all human cancers involve p53 mutations,which occur mostly in the sequence-specific DNA-binding central domain (p53c), yielding little/non-detectable af?nity to the DNA consensus site. Despite our current understanding of protein-DNA recognition,the mechanism(s) underlying the loss in protein-DNA binding afnity/ specificity upon single-point mutation are not well understood. Our goal is to identify the common factors governing the DNA-binding loss of p53c upon substitution of Arg 273 to His or Cys,which are abundant in human tumours. By computing the free energies of wild-type and mutant p53c binding to DNA and decomposing them into contributions from individual residues, the DNA-binding loss upon charge/noncharge -conserving mutation of Arg 273 was attributed not only to the loss of DNA phosphate contacts, but also to longer-range structural changes caused by the loss of the Asp 281 salt-bridge. The results herein and in previous works suggest that Asp 281 plays a critical role in the sequence-specific DNA-binding function of p53c by (i)orienting Arg 273 and Arg 280 in an optimal position to interact with the phosphate and base groups of the consensus DNA, respectively, and (ii) helping to maintain the proper DNA-binding protein conformation.
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