Abstract
The design of a broad-spectrum cancer drug would provide enormous clinical benefits to treat cancer patients. Most of cancerous cells have a mutation in the p53 gene that results in an inactive mutant p53 protein. For this reason, p53 is a prime target for the development of a broad-spectrum cancer drug. To provide the atomic information to rationally design a drug to recover p53 activity is the main goal of the structural studies on mutant p53. We review three mechanisms that influence p53 activity and provide information about how reactivation of mutant p53 can be achieved: stabilization of the active conformation of the DNA-binding domain of the protein, suppression of missense mutations in the DNA-binding domain by a second- site mutation, and increased transactivation.
Original language | English |
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Pages (from-to) | 119-132 |
Number of pages | 14 |
Journal | Sub-Cellular Biochemistry |
Volume | 85 |
DOIs | |
Publication status | Published - 2014 |
Keywords
- Crystallography
- Mutant p53
- p53 activation
- p53 structure
- p53 transactivation
- Suppression p53 missense mutations
ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Cancer Research
- Molecular Biology
- Medicine(all)