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Modelling the interaction between the p53 DNA-binding domain and the p28 peptide fragment of Azurin by Simona Santini; Anna Rita Bizzarri; Salvatore Cannistraro is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Modelling the interaction between the p53 DNA-binding domain and the p28 peptide fragment of Azurin about?

Recent experimental data reveal that the peptide fragment of Azurin called p28, constituted by the amino acid residues from 50 to 77 of the whole protein, retains both the Azurin cellular penetration ability and antiproliferative activity. p28 is hypothesized to act by stabilizing the well‐known tumour suppressor p53 via a pathway independent from the oncogene Mdm2, which is the main p53 down‐regulator, with its anticancer potentiality being probably connected with the binding of its amino acid residues 11 to 18 to p53. However, the p28 mode of action has not been completely elucidated yet, mostly because the details of the p28 interaction with p53 are still unknown. In the present study, computational docking modelling supported by cluster analysis, molecular dynamics simulations and binding free energy calculations have been performed to model the interaction between the DNA‐binding domain (DBD) of p53 and the p28 fragment. Since the folding state of p28 when interacting with p53 inside the cell is not known, both the folded and the unfolded structures of this peptide have been taken into consideration. In both the cases, we have found that p28 is able to form with DBD a complex

Who reads Modelling the interaction between the p53 DNA-binding domain and the p28 peptide fragment of Azurin?

Author

Simona Santini; Anna Rita Bizzarri; Salvatore Cannistraro

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0952-3499)

Published

2011

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)