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- W2051355276 abstract "Molecular interaction between p53 tumor suppressor and the copper protein azurin (AZ) has been demonstrated to enhance p53 stability and hence antitumoral function, opening new perspectives in cancer treatment. While some experimental work has provided evidence for AZ binding to p53, no crystal structure for the p53-AZ complex was solved thus far. In this work the association between AZ and the p53 DNA-binding domain (DBD) was investigated by computational methods. Using a combination of rigid-body protein docking, experimental mutagenesis information, and cluster analysis 10 main p53 DBD-AZ binding modes were generated. The resulting structures were further characterized by molecular dynamics (MD) simulations and free energy calculations. We found that the highest scored docking conformation for the p53 DBD-AZ complex also yielded the most favorable free energy value. This best three-dimensional model for the complex was validated by using a computational mutagenesis strategy. In this structure AZ binds to the flexible L(1) and s(7)-s(8) loops of the p53 DBD and stabilizes them through protein-protein tight packing interactions, resulting in high degree of both surface matching and electrostatic complementarity." @default.
- W2051355276 created "2016-06-24" @default.
- W2051355276 creator A5034858646 @default.
- W2051355276 creator A5036589086 @default.
- W2051355276 creator A5039099214 @default.
- W2051355276 date "2007-07-01" @default.
- W2051355276 modified "2023-10-18" @default.
- W2051355276 title "Docking study and free energy simulation of the complex between p53 DNA‐binding domain and azurin" @default.
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- W2051355276 doi "https://doi.org/10.1002/jmr.840" @default.
- W2051355276 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17703463" @default.
- W2051355276 hasPublicationYear "2007" @default.
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