Crystallographic analysis of an 8-mer p53 peptide analogue complexed with MDM2

Journal of the American Chemical Society

Volumn 128, Issue 34, 2006, Pages 11000-11001

  Sakurai, Kaori ^a   Schubert, Carsten ^b   Kahne, Daniel ^a,c  

^a HARVARD UNIVERSITY   (United States)

^b JOHNSON AND JOHNSON PHARMACEUTICAL RESEARCH AND DEVELOPMENT   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; PEPTIDE DERIVATIVE; PROTEIN MDM2; PROTEIN P53;

AMINO ACID SEQUENCE; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROPHOBICITY; IC 50; MOLECULAR INTERACTION; PEPTIDE SYNTHESIS; PREDICTION; PROTEIN BINDING; PROTEIN FUNCTION; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTO-ONCOGENE PROTEINS C-MDM2; TUMOR SUPPRESSOR PROTEIN P53;

EID: 33748076161     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja063102j     Document Type: Article

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25. Two rotamers around the C-P bond observed for the phosphonate groups in the complex, respectively, make different patterns of water-mediated hydrogen bonds to the MDM2 residues (Figure S3). Although unlikely, we cannot exclude the possibility that they may contribute to the increased stabilization of the MDM2-peptide interaction.
26. Coordinates for the structure have been deposited with the RCSB Protein Data Bank (PDB access code 2GV2).