Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations.

Abstract excerpt

We have solved the crystal structures of three oncogenic mutants of the core domain of the human tumor suppressor p53. The mutations were introduced into a stabilized variant. The cancer hot spot mutation R273H simply removes an arginine involved in DNA binding without causing structural distortions in neighboring residues. In contrast, the "structural" oncogenic mutations H168R and R249S induce substantial...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Arginine
• Share to Cancer-related Molecular Pathways