Article
The electrostatic surface of MDM2 modulates the specificity of its interaction with phosphorylated and unphosphorylated p53 peptides.
Cell cycle (Georgetown, Tex.) - 1 Mar 2008
Brown Christopher John, Srinivasan Deepa, Jun Lee Hui, Coomber David, Verma Chandra S, Lane David P
Abstract excerpt
Florescence anisotropy measurements using FAM-labelled p53 peptides showed that the binding of the peptides to MDM2 was dependant upon the phosphorylation of p53 at Thr18 and that this binding was modulated by the electrostatic properties of MDM2. In agreement with computational predictions, the binding to phosphorylated p53 peptide, in comparison to the unphosphorylated p53 peptide, was enhanced upon mutation of...
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