How Do Cancer-Related Mutations Affect the Oligomerisation State of the p53 Tetramerisation Domain?

ABSTRACT: Tumour suppressor p53 plays a key role in the development of cancer and has therefore been widely studied in recent decades. While it is well known that p53 is biologically active as a tetramer, the tetramerisation mechanism is still not completely understood. p53 is mutated in nearly 50% of cancers, and mutations can alter the oligomeric state of the protein, having an impact on the biological function of the protein and on cell fate decisions. Here, we describe the effects of a number of representative cancer-related mutations on tetramerisation domain (TD) oligomerisation defining a peptide length that permits having a folded and structured domain, thus avoiding the effect of the flanking regions and the net charges at the N- and C-terminus. These peptides have been studie

SUBMITTER: Nicolini F 

PROVIDER: S-EPMC10296842 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature