MD simulations on the structure of onco-proteins p53: Wild-type and radioresistant mutant systems

Kholmirzo T. Kholmurodov, Evgenii A. Krasavin, Viktor A. Krylov, Ermuhammad B. Dushanov, Vladimir V. Korenkov, Kenji Yasuoka, Tetsu Narumi, Yousuke Ohno, Makoto Taiji, Toshikazu Ebisuzaki

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Based on molecular dynamics (MD) simulation, a comparative analysis has been performed of the p53 dimer - DNA interaction for the wildtype and mutant Arg273His (R273H) proteins. The aim of this paper is to study the molecular mechanism of the p53 onco-protein and DNA binding. A comparative analysis shows that the R273H mutation has a significant effect on the p53-DNA interaction removing their close contact. The obtainedMD simulation results illustrate in detail the molecular mechanism of the conformations of the key amino acids in the p53-DNA binding domain, which is important for the physiological functioning of the p53 protein and understanding the origin of cancer.

Original languageEnglish
Title of host publicationMolecular Dynamics of Nanobiostructures
PublisherNova Science Publishers, Inc.
Pages179-208
Number of pages30
ISBN (Print)9781613243206
Publication statusPublished - 2013 Jan 1

Keywords

  • MD simulations
  • Onco-protein p53
  • P53r273h mutation

ASJC Scopus subject areas

  • Chemical Engineering(all)
  • Physics and Astronomy(all)
  • Chemistry(all)

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    Kholmurodov, K. T., Krasavin, E. A., Krylov, V. A., Dushanov, E. B., Korenkov, V. V., Yasuoka, K., Narumi, T., Ohno, Y., Taiji, M., & Ebisuzaki, T. (2013). MD simulations on the structure of onco-proteins p53: Wild-type and radioresistant mutant systems. In Molecular Dynamics of Nanobiostructures (pp. 179-208). Nova Science Publishers, Inc..