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.
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Titolo: | Structural studies on mechanisms to activate mutant p53. |
Autori: | H., Viadiu; G., Fronza; Inga, Alberto |
Autori Unitn: | |
Titolo del volume contenente il saggio: | Subcellular Biochemistry series |
Luogo di edizione: | Springer Dordrecht Heidelberg New York London |
Casa editrice: | Springer |
Anno di pubblicazione: | 2014 |
Handle: | http://hdl.handle.net/11572/100835 |
Appare nelle tipologie: | 02.1 Saggio su volume miscellaneo o Capitolo di libro (Essay or Book Chapter) |