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IMAGE: A model produced by scientists at Rice University shows the conformational changes caused by a mutation in the cancer-fighting p53 protein. At top left, the red box highlights the aggregation-prone. view more
Credit: Kolomeisky Research Group/Rice University
HOUSTON - (March 4, 2021) - A mutation that replaces a single amino acid in a potent tumor-suppressing protein turns it from saint to sinister. A new study by a coalition of Texas institutions shows why that is more damaging than previously known.
The ubiquitous p53 protein in its natural state, sometimes called the guardian of the genome, is a front-line protector against cancer. But the mutant form appears in 50% or more of human cancers and actively blocks cancer suppressors.