Technical Articles

This article focuses on the molecular characteristics and druggability basis of the p53 Y220C mutant protein, systematically elaborating its unique mechanism of action as a structural mutation-type hotspot mutation that distinguishes it from contact mutations, analyzing the structural basis by which this mutation creates an extended surface crevice on the surface of the p53 protein DNA-binding domain and leads to thermodynamic instability, and exploring the structural rationale provided by this crevice as a small-molecule druggable pocket for the design of specific stabilizers.