期刊
CELL CYCLE
卷 7, 期 5, 页码 608-610出版社
TAYLOR & FRANCIS INC
DOI: 10.4161/cc.7.5.5488
关键词
MDM2; p53; phosphorylation; fluorescence; electrostatics; mutant; affinity
类别
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.
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