2GV2

MDM2 in complex with an 8-mer p53 peptide analogue

Summary for 2GV2

• Entry DOI: 10.2210/pdb2gv2/pdb
• Related: 1RV1 1T4E 1T4F 1YCR
• Descriptor: E3 ubiquitin-protein ligase Mdm2, 8-MER P53 PEPTIDE ANALOGUE (3 entities in total)
• Functional Keywords: optimized protein-protein interaction. synthetic peptide. alpha helix binding protein, ligase
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus, nucleoplasm: Q00987
• Total number of polymer chains: 2
• Total formula weight: 13787.12

Authors

Schubert, C.,Sakurai, K. (deposition date: 2006-05-02, release date: 2006-09-05, Last modification date: 2023-11-15)

Primary citation

Sakurai, K.,Schubert, C.,Kahne, D.
Crystallographic Analysis of an 8-mer p53 Peptide Analogue Complexed with MDM2.
J.Am.Chem.Soc., 128:11000-11001, 2006

PubMed Abstract: 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.

PubMed: 16925398
DOI: 10.1021/ja063102j

Experimental method

X-RAY DIFFRACTION (1.8 Å)