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2ioi

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[[Image:2ioi.gif|left|200px]]
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{{STRUCTURE_2ioi| PDB=2ioi | SCENE= }}
{{STRUCTURE_2ioi| PDB=2ioi | SCENE= }}
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'''Crystal structure of the mouse p53 core domain at 1.55 A'''
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===Crystal structure of the mouse p53 core domain at 1.55 A===
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==Overview==
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The p53 transcriptional regulator is the most frequently mutated protein in human cancers and the majority of tumor-derived p53 mutations map to the central DNA-binding core domain, with a subset of these mutations resulting in reduced p53 stability. Here, the 1.55 A crystal structure of the mouse p53 core domain with a molecule of tris(hydroxymethyl)aminomethane (Tris) bound through multiple hydrogen bonds to a region of p53 shown to be important for repair of a subset of tumor-derived p53-stability mutations is reported. Consistent with the hypothesis that Tris binding stabilizes the p53 core domain, equilibrium denaturation experiments are presented that demonstrate that Tris binding increases the thermodynamic stability of the mouse p53 core domain by 3.1 kJ mol(-1) and molecular-dynamic simulations are presented revealing an overall reduction in root-mean-square deviations of the core domain of 0.7 A when Tris is bound. It is also shown that these crystals of the p53 core domain are suitable for the multiple-solvent crystal structure approach to identify other potential binding sites for possible core-domain stabilization compounds. Analysis of the residue-specific temperature factors of the high-resolution core-domain structure, coupled with a comparison with other core-domain structures, also reveals that the L1, H1-S5 and S7-S8 core-domain loops, also shown to mediate various p53 activities, harbor inherent flexibility, suggesting that these regions might be targets for other p53-stabilizing compounds. Together, these studies provide a molecular scaffold for the structure-based design of p53-stabilization compounds for development as possible therapeutic agents.
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(as it appears on PubMed at http://www.pubmed.gov), where 17139084 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17139084}}
==About this Structure==
==About this Structure==
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[[Category: Zhao, K.]]
[[Category: Zhao, K.]]
[[Category: Ig fold]]
[[Category: Ig fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:43:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:29:52 2008''

Revision as of 00:29, 28 July 2008

Image:2ioi.png

Template:STRUCTURE 2ioi

Crystal structure of the mouse p53 core domain at 1.55 A

Template:ABSTRACT PUBMED 17139084

About this Structure

2IOI is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

High-resolution structure of the p53 core domain: implications for binding small-molecule stabilizing compounds., Ho WC, Luo C, Zhao K, Chai X, Fitzgerald MX, Marmorstein R, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1484-93. Epub 2006, Nov 23. PMID:17139084

Page seeded by OCA on Mon Jul 28 03:29:52 2008

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