Cell Cycle. 2008 Mar 1;7(5):608-10. Epub 2007 Dec 26.

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

Brown CJ, Srinivasan D, Jun LH, Coomber D, Verma CS, Lane DP.

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Laboratory of Cell Cycle Control, Institute of Molecular and Cell Biology, Singapore.

Abstract

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.

PMID:: 18256546; [PubMed - indexed for MEDLINE]

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

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