Article
Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells.
Nature chemical biology - 1 Dec 2014
Borcherds Wade, Theillet François-Xavier, Katzer Andrea, Finzel Ana, Mishall Katie M, Powell Anne T, Wu Hongwei, Manieri Wanda, Dieterich Christoph, Selenko Philipp, Loewer Alexander, Daughdrill Gary W
Abstract excerpt
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...
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