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Brief Report

The electrostatic surface of MDM2 modulates the specificity of its interaction with phosphorylated and unphosphorylated p53 peptides

Christopher John Brown, Deepa Srinivasan, Lee Hui Jun, David Coomber, Chandra S. Verma and David P. Lane

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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 3 key residues on the MDM2 surface.

Authors

Christopher John Brown

Institute of Molecular and Cell Biology; Proteos, Singapore

Deepa Srinivasan

Institute of Molecular and Cell Biology; Proteos, Singapore

Lee Hui Jun

Bioinformatics Institute; Matrix, Singapore

David Coomber

Institute of Molecular and Cell Biology; Proteos, Singapore

Chandra S. Verma

Bioinformatics Institute; Matrix, Singapore

David P. Lane

Institute for Molecular and Cellular Biology; Proteos, Singapore

Purchase article for $19

Subscribe to this journal for $129/year