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

Pub. Date : 2008 Mar 1

PMID : 18256546






2 Functional Relationships(s)
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1 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. UNII-PYZ33YLR8A tumor protein p53 Homo sapiens
2 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. UNII-PYZ33YLR8A tumor protein p53 Homo sapiens