1uol
From Proteopedia
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CRYSTAL STRUCTURE OF THE HUMAN P53 CORE DOMAIN MUTANT M133L/V203A/N239Y/N268D AT 1.9 A RESOLUTION.
Overview
Most of the cancer-associated mutations in the tumor suppressor p53 map to, its DNA-binding core domain. Many of them inactivate p53 by decreasing its, thermodynamic stability. We have previously designed the superstable, quadruple mutant M133L/V203A/N239Y/N268D containing the second-site, suppressor mutations N239Y and N268D, which specifically restore activity, and stability in several oncogenic mutants. Here we present the x-ray, structure of this quadruple mutant at 1.9 A resolution, which was solved, in a new crystal form in the absence of DNA. This structure reveals that, the four point mutations cause only small local structural changes, whereas the overall structure of the central beta-sandwich and the, DNA-binding surface is conserved. The suppressor mutation N268D results in, an ... [(full description)]
About this Structure
1UOL is a [Single protein] structure of sequence from [Homo sapiens] with ZN as [ligand]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations., Joerger AC, Allen MD, Fersht AR, J Biol Chem. 2004 Jan 9;279(2):1291-6. Epub 2003 Oct 8. PMID:14534297
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