Structure analysis of a p53 fusion protein

Michael Landreh
The tumor suppressor p53 is a key target for cancer therapy, but its low expression levels, poor conformational stability, and high degree of disorder remain major challenges to its structural investigation. Here, we address these issues by fusing the N-terminal transactivation domain of p53 to an engineered spider silk domain termed NT*. Molecular dynamics simulations show that the disordered transactivation domain of p53 wraps around the NT* domain via a series of folding events, resulting...
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