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The crystal structure of the R280K mutant of human p53 explains the loss of DNA binding

  • Gomes, Ana Sara; Trovão, Filipa; Andrade Pinheiro, Benedita; Freire, Filipe; Gomes, Sara; Oliveira, Carla; Domingues, Lucília; Romão, Maria João; Saraiva, Lucília; Carvalho, Ana Luísa
  • International Journal of Molecular Sciences, 19(4), 1184, 2018

Publisher: MDPI Open Access Publishing

Abstract

The p53 tumor suppressor is widely found to be mutated in human cancer. This protein is regarded as a molecular hub regulating different cell responses, namely cell death. Compelling data have demonstrated that the impairment of p53 activity correlates with tumor development and maintenance. For these reasons, the reactivation of p53 function is regarded as a promising strategy to halt cancer. In the present work, the recombinant mutant p53R280K DNA binding domain (DBD) was produced for the first time, and its crystal structure was determined in the absence of DNA to a resolution of 2.0 Å. The ...

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