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.; Wu, H.; Manieri, W.; Dieterich, C.; Selenko, P.; Loewer, A.; Daughdrill, G. W.

doi:10.1038/nchembio.1668

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

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Dieterich, C.
Dieterich – Computational RNA Biology and Ageing, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

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http://www.ncbi.nlm.nih.gov/pubmed/25362358
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Citation

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.

Cite as: https://hdl.handle.net/21.11116/0000-000B-B34C-6

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.