2j20
From Proteopedia
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HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-N239Y-N268D-R273C
Overview
The DNA-binding domain of the tumor suppressor p53 is inactivated by, mutation in approximately 50% of human cancers. We have solved, high-resolution crystal structures of several oncogenic mutants to, investigate the structural basis of inactivation and provide information, for designing drugs that may rescue inactivated mutants. We found a, variety of structural consequences upon mutation: (i) the removal of an, essential contact with DNA, (ii) creation of large, water-accessible, crevices or hydrophobic internal cavities with no other structural changes, but with a large loss of thermodynamic stability, (iii) distortion of the, DNA-binding surface, and (iv) alterations to surfaces not directly, involved in DNA binding but involved in domain-domain interactions on, binding as a ... [(full description)]
About this Structure
2J20 is a [Single protein] structure of sequence from [Homo sapiens] with ZN and SO4 as [ligands]. Full crystallographic information is available from [OCA].
Reference
Structural basis for understanding oncogenic p53 mutations and designing rescue drugs., Joerger AC, Ang HC, Fersht AR, Proc Natl Acad Sci U S A. 2006 Oct 10;103(41):15056-61. Epub 2006 Oct 2. PMID:17015838
Page seeded by OCA on Mon Oct 29 16:10:48 2007
Categories: Homo sapiens | Single protein | Ang, H.C. | Fersht, A.R. | Joerger, A.C. | SO4 | ZN | Acetylation | Activator | Alternative splicing | Anti-oncogene | Apoptosis | Cell cycle | Disease mutation | Dna-binding | Dna-binding protein | Glycoprotein | Host-virus interaction | Li-fraumeni syndrome | Metal-binding | Nuclear protein | P53 dna-binding domain | Phosphorylation | Polymorphism | Second-site suppressor mutation | Superstable mutant | Transcription | Transcription regulation | Transferase | Tumor suppressor | Zinc
