Structure of the negative regulatory domain of p53 bound to S100B(betabeta).

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TitleStructure of the negative regulatory domain of p53 bound to S100B(betabeta).
Publication TypeJournal Article
Year of Publication2000
AuthorsRustandi, RR, Baldisseri, DM, Weber, DJ
JournalNat Struct Biol
Volume7
Issue7
Pagination570-4
Date Published2000 Jul
ISSN1072-8368
KeywordsAcetylation, Apoproteins, Binding Sites, Calcium, Calcium-Binding Proteins, Dimerization, Humans, Models, Molecular, Molecular Sequence Data, Nerve Growth Factors, Nuclear Magnetic Resonance, Biomolecular, Peptide Fragments, Phosphorylation, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, S100 Proteins, Static Electricity, Tumor Suppressor Protein p53
Abstract

A Ca2+ dependent conformational change in dimeric S100B(betabeta) is required for it to bind p53 and inhibit phosphorylation of this tumor suppressor in its C-terminal negative regulatory domain. A peptide derived from this region of p53 (residues 367-388) was found to have no regular structure in its native form by NMR spectroscopy, but becomes helical when bound to Ca2+ loaded S100B(betabeta). The three-dimensional structure of this complex reveals several favorable hydrophobic and electrostatic interactions between S100B(betabeta) and the p53 peptide in the binding pocket, where S100B(betabeta) sterically blocks sites of phosphorylation and acetylation on p53 that are important for transcription activation.

DOI10.1038/76797
Alternate JournalNat. Struct. Biol.
PubMed ID10876243