2gv2: Difference between revisions

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{{STRUCTURE_2gv2|  PDB=2gv2  |  SCENE=  }}  
{{STRUCTURE_2gv2|  PDB=2gv2  |  SCENE=  }}  


'''MDM2 in complex with an 8-mer p53 peptide analogue'''
===MDM2 in complex with an 8-mer p53 peptide analogue===




==Overview==
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The most potent inhibitor of the p53-MDM2 interaction reported to date is an 8-mer p53 peptide analogue (Novartis peptide), which contains 6-chlorotryptophane (Cl-Trp) and phosphonomethylphenylalanine (Pmp) as key residues for the enhanced activity. We report here a crystal structure of the co-complex between MDM2 and the Novartis peptide solved at 1.8 A resolution. The structural basis for the role of the two aromatic residues are delineated by comparing the present structure with crystal structures of the MDM2 co-complex bound to other inhibitors including the wt-p53 peptide itself.
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{{ABSTRACT_PUBMED_16925398}}


==About this Structure==
==About this Structure==
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[[Category: Schubert, C.]]
[[Category: Schubert, C.]]
[[Category: Optimized protein-protein interaction. synthetic peptide. alpha helix binding protein]]
[[Category: Optimized protein-protein interaction. synthetic peptide. alpha helix binding protein]]
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