期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 13, 期 8, 页码 9709-9740出版社
MDPI AG
DOI: 10.3390/ijms13089709
关键词
p53; MDM2; MDMX; molecular dynamic simulation; conformational change; protein-protein interaction; protein-ligand interaction
资金
- National Natural Science Foundation of China [31070641]
- National Basic Research Program of China [2012CB721002]
- Chinese Academy of Sciences
As a tumor suppressor protein, p53 plays a crucial role in the cell cycle and in cancer prevention. Almost 50 percent of all human malignant tumors are closely related to a deletion or mutation in p53. The activity of p53 is inhibited by over-active celluar antagonists, especially by the over-expression of the negative regulators MDM2 and MDMX. Protein-protein interactions, or post-translational modifications of the C-terminal negative regulatory domain of p53, also regulate its tumor suppressor activity. Restoration of p53 function through peptide and small molecular inhibitors has become a promising strategy for novel anti-cancer drug design and development. Molecular dynamics simulations have been extensively applied to investigate the conformation changes of p53 induced by protein-protein interactions and protein-ligand interactions, including peptide and small molecular inhibitors. This review focuses on the latest MD simulation research, to provide an overview of the current understanding of interactions between p53 and its partners at an atomic level.
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