The electrostatic surface of MDM2 modulates the specificity of its interaction with phosphorylated and unphosphorylated p53 peptides

Cell Cycle

Volumn 7, Issue 5, 2008, Pages 608-610

  Brown, Christopher John ^a   Srinivasan, Deepa ^a   Lee, Hui Jun ^b   Coomber, David ^a   Verma, Chandra S ^b   Lane, David P ^a  

^a INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Singapore)

^b BIOINFORMATICS INSTITUTE   (Singapore)

Author keywords

Affinity; Electrostatics; Fluorescence; MDM2; Mutant; p53; Phosphorylation

Indexed keywords

ASPARTIC ACID; GLUTAMINE; PEPTIDE; PHENYLALANINE; PROTEIN MDM2; PROTEIN P53; TYROSINE; UBIQUITIN PROTEIN LIGASE E3;

AMINO TERMINAL SEQUENCE; ANISOTROPY; ARTICLE; BINDING AFFINITY; BINDING KINETICS; CELL CYCLE ARREST; COMPARATIVE STUDY; ELECTRICITY; FLUORESCENCE MICROSCOPE; GENE MUTATION; MOLECULAR INTERACTION; PLASMID; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; SURFACE PROPERTY; TUMOR SUPPRESSOR GENE;

EID: 38949135781     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.7.5.5488     Document Type: Article

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