期刊
NATURE CHEMICAL BIOLOGY
卷 10, 期 12, 页码 1000-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.1668
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资金
- Deutsche Forschungsgemeinschaft [PS1794/1-1]
- Association pour la Recherche contre le Cancer
- European Union FP7
- American Cancer Society [RSG-07-289-01-GMC]
- National Science Foundation [MCB-0939014]
- Center for Drug Discovery and Innovation
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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