2bio
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HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-N239Y-R249S-N268D
OverviewOverview
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, structural perturbation around the mutation site in the L2 and L3 loops, respectively. H168R is a specific intragenic suppressor mutation for, R249S. When both cancer mutations are combined in the same molecule, Arg(168) mimics the role of Arg(249) in wild type, and the wild type, conformation is largely restored in both loops. Our structural and, biophysical data provide ... [(full description)]
About this StructureAbout this Structure
2BIO is a [Single protein] structure of sequence from [Homo sapiens] with ZN as [ligand]. Full crystallographic information is available from [OCA].
ReferenceReference
Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations., Joerger AC, Ang HC, Veprintsev DB, Blair CM, Fersht AR, J Biol Chem. 2005 Apr 22;280(16):16030-7. Epub 2005 Feb 9. PMID:15703170
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- Homo sapiens
- Single protein
- Fersht, A.R.
- Joerger, A.C.
- ZN
- 3d-structure
- Activator
- Anti-oncogene
- Apoptosis
- Disease mutation
- Dna-binding
- Dna-binding protein
- Li-fraumeni syndrome
- Nuclear protein
- P53 dna-binding domain
- Phosphorylation
- Polymorphism
- Second-site suppressor mutation
- Superstable mutant
- Transcription regulation
- Tumor suppressor