Disorder and Residual Helicity Alter p53-Mdm2 Binding Affinity and Signaling in Cells
Document Type
Article
Publication Date
2014
Keywords
Biochemistry, Cancer, Cell Signalling, NMR Spectroscopy
Digital Object Identifier (DOI)
https://doi.org/10.1038/nchembio.1668
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.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Nature Chemical Biology, v. 10, p. 1000-1002
Scholar Commons Citation
Borcherds, Wade M.; Theillet, Francois-Xavier; Katzer, Andrea; Finzel, Ana; Mishall, Katie M.; Powell, Anne T.; Wu, Hongwei; Manieri, Wanda; Dieterich, Christoph; Selenko, Philipp; Loewer, Alexander; and Daughdrill, Gary W., "Disorder and Residual Helicity Alter p53-Mdm2 Binding Affinity and Signaling in Cells" (2014). Molecular Biosciences Faculty Publications. 165.
https://digitalcommons.usf.edu/bcm_facpub/165
