The electrostatic surface of MDM2 modulates the specificity of its interaction with phosphorylated and unphosphorylated p53 peptides
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 bin...
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| Veröffentlicht in: | Cell cycle (Georgetown, Tex.) Tex.), 2008-03, Vol.7 (5), p.608-610 |
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| creator | Brown, Christopher John Srinivasan, Deepa Jun, Lee Hui Coomber, David Verma, Chandra S Lane, David P |
| description | 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. |
| doi_str_mv | 10.4161/cc.7.5.5488 |
| format | Article |
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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.</abstract><cop>United States</cop><pmid>18256546</pmid><doi>10.4161/cc.7.5.5488</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Cell cycle (Georgetown, Tex.), 2008-03, Vol.7 (5), p.608-610 |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals |
| subjects | Binding Biology Bioscience Calcium Cancer Cell Crystallography, X-Ray Cycle Fluorescence Polarization Landes Models, Molecular Mutation - genetics Organogenesis Phosphopeptides - metabolism Phosphorylation Protein Binding Proteins Proto-Oncogene Proteins c-mdm2 - chemistry Proto-Oncogene Proteins c-mdm2 - metabolism Static Electricity Structure-Activity Relationship Tumor Suppressor Protein p53 - chemistry Tumor Suppressor Protein p53 - metabolism |
| title | The electrostatic surface of MDM2 modulates the specificity of its interaction with phosphorylated and unphosphorylated p53 peptides |
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