Structures of p53 Cancer Mutants and Mechanism of Rescue by Second-site Suppressor Mutations

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...

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Veröffentlicht in:	The Journal of biological chemistry 2005-04, Vol.280 (16), p.16030-16037
Hauptverfasser:	Joerger, Andreas C., Ang, Hwee Ching, Veprintsev, Dmitry B., Blair, Caroline M., Fersht, Alan R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Arginine - genetics Arginine - metabolism Crystallography, X-Ray DNA - metabolism Humans Mutation Protein Binding Protein Structure, Tertiary Tumor Suppressor Protein p53 - chemistry Tumor Suppressor Protein p53 - genetics
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