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| Item Type: | Article |
|---|---|
| Title: | Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells |
| Creators Name: | Borcherds, W. and Theillet, F.X. and Katzer, A. and Finzel, A. and Mishall, K.M. and Powell, A.T. and Wu, H. and Manieri, W. and Dieterich, C. and Selenko, P. and Loewer, A. and Daughdrill, G.W. |
| 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. |
| Keywords: | Cell Cycle, Tumor Cell Line, DNA Damage, Escherichia coli, Gamma Rays, Gene Expression Regulation, Intrinsically Disordered Proteins, Molecular Models, Mutation, Protein Folding, Proto-Oncogene Proteins c-mdm2, Recombinant Proteins, Secondary Protein Structure, Signal Transduction, Tertiary Protein Structure, Tumor Suppressor Protein p53 |
| Source: | Nature Chemical Biology |
| ISSN: | 1552-4450 |
| Publisher: | Nature Publishing Group |
| Volume: | 10 |
| Number: | 12 |
| Page Range: | 1000-1002 |
| Date: | December 2014 |
| Official Publication: | https://doi.org/10.1038/nchembio.1668 |
| PubMed: | View item in PubMed |
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