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Pearlman, D.A., Case, D.A., Caldwell, J.W., Ross, W.R., Cheatham, T.E., DeBolt, S., Ferguson, D., Seibel, G., Kollman, P., “AMBER, a computer program for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to elucidate the structures and energies of molecules”. Comp. Phys. Commun., 91, 1995, 1-41.

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• TITLE: MD Simulations of the P53 oncoprotein structure: the effect of the Arg273→His mutation on the DNA binding domain

  AUTHORS: Kholmirzo Kholmurodov, Ermuhammad Dushanov, Kenji Yasuoka

  KEYWORDS: Molecular Dynamics Simulations; p53 Oncoprotein; Effect of the R273H Mutation; DNA Binding Domain

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.2 No.5, October 13, 2011

  ABSTRACT: A comparative molecular dynamics (MD) simulation study was performed on the p53 oncoprotein to investigate the effect of the Arg273His (R273H) mutation on the p53→DNA Binding Domain (DBD). The two p53 dimer structures of the wild-type and mutant Arg273His (R273H) were simulated with the same thermodynamic and environmental parameters. The obtained results demonstrate that the induced Arg273His mutation has a considerable effect on the p53→DNA close contact interaction and changes the picture of hydrogen formation. The Arg273His mutation, in some cases, destroys the existing native hydrogen bond, but, in other cases, forms a strong p53→DNA hydrogen bond, which is not proper for the native protein. The MD simulation results illustrate some molecular mechanism of the conformational changes of the Arg273His key amino acid residue in the p53→DNA binding domain, which might be important for the understanding of the physiological functioning of the p53 protein and the origin of cancer.