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  Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells

Borcherds, W., Theillet, F. X., Katzer, A., Finzel, A., Mishall, K. M., Powell, A. T., et al. (2014). Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells. Nat Chem Biol, 10(12), 1000-2. doi:10.1038/nchembio.1668.

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Borcherds, W., Author
Theillet, F. X., Author
Katzer, A., Author
Finzel, A., Author
Mishall, K. M., Author
Powell, A. T., Author
Wu, H., Author
Manieri, W., Author
Dieterich, C.1, Author           
Selenko, P., Author
Loewer, A., Author
Daughdrill, G. W., Author
Affiliations:
1Dieterich – Computational RNA Biology and Ageing, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_1942300              

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Free keywords: Cell Cycle/genetics/radiation effects Cell Line, Tumor DNA Damage Escherichia coli/genetics/metabolism Gamma Rays Gene Expression Regulation Humans Intrinsically Disordered Proteins/*chemistry/genetics/metabolism Models, Molecular Mutation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Proto-Oncogene Proteins c-mdm2/*chemistry/genetics/metabolism Recombinant Proteins/chemistry/genetics/metabolism *Signal Transduction Tumor Suppressor Protein p53/*chemistry/genetics/metabolism
 Abstract: Levels of residual structure in disordered interaction domains determine in vitro binding affinities, but whether they exert similar roles in cells is not known. Here, we show that increasing residual p53 helicity results in stronger Mdm2 binding, altered p53 dynamics, impaired target gene expression and failure to induce cell cycle arrest upon DNA damage. These results establish that residual structure is an important determinant of signaling fidelity in cells.

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 Dates: 2014
 Publication Status: Issued
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 Identifiers: DOI: 10.1038/nchembio.1668
ISSN: 1552-4469 (Electronic)1552-4450 (Linking)
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Title: Nat Chem Biol
Source Genre: Journal
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Pages: - Volume / Issue: 10 (12) Sequence Number: - Start / End Page: 1000 - 2 Identifier: -