ArticleInternational journal of molecular sciences2010
Insight into a novel p53 single point mutation (G389E) by Molecular Dynamics Simulations.
Article in International journal of molecular sciences, 2010. 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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13 citing papers in PubMed, 21 citations in OpenAlex.
- Assessing the Performance of BioEmu in Understanding Protein Dynamics.International journal of molecular sciences · 2026Article
- Molecular Dynamics Investigations of Human DNA-Topoisomerase I Interacting with Novel Dewar Valence Photo-Adducts: Insights into Inhibitory Activity.International journal of molecular sciences · 2023Article
- KLF7: a new candidate biomarker and therapeutic target for high-grade serous ovarian cancer.Journal of experimental & clinical cancer research : CR · 2020Article
- Identification and Modeling of a GT-A Fold in the α-Dystroglycan Glycosylating Enzyme LARGE1.Journal of chemical information and modeling · 2020Article
- Article
- A novel dysfunctional germline P53 mutation identified in a family with Li-Fraumeni syndrome.American journal of cancer research · 2018Article
- Human Aquaporin-4 and Molecular Modeling: Historical Perspective and View to the Future.International journal of molecular sciences · 2016Review
- Long range recognition and selection in IDPs: the interactions of the C-terminus of p53.Scientific reports · 2016Article
- Article
- Computational studies of difference in binding modes of peptide and non-peptide inhibitors to MDM2/MDMX based on molecular dynamics simulations.International journal of molecular sciences · 2012Article
- Binding of two intrinsically disordered peptides to a multi-specific protein: a combined Monte Carlo and molecular dynamics study.PLoS computational biology · 2012Article
- Molecular dynamic simulation insights into the normal state and restoration of p53 function.International journal of molecular sciences · 2012Review
- The road from next-generation sequencing to personalized medicine.Personalized medicineArticle
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The majority of inactivating mutations of p53 reside in the central core DNA binding domain of the protein. In this computational study, we investigated the structural effects of a novel p53 mutation (G389E), identified in a patient with congenital adrenal hyperplasia, which is located within the extreme C-terminal domain (CTD) of p53, an unstructured, flexible region (residues 367-393) of major importance for the regulation of the protein. Based on the three-dimensional structure of a carboxyl-terminal peptide of p53 in complex with the S100B protein, which is involved in regulation of the tumor suppressor activity, a model of wild type (WT) and mutant extreme CTD was developed by molecular modeling and molecular dynamics simulation. It was found that the G389E amino acid replacement has negligible effects on free p53 in solution whereas it significantly affects the interactions of p53 with the S100B protein. The results suggest that the observed mutation may interfere with p53 transcription activation and provide useful information for site-directed mutagenesis experiments.
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