S100B(betabeta) inhibits the protein kinase C-dependent phosphorylation of a peptide derived from p53 in a Ca2+-dependent manner.

@article{Wilder1998S100BbetabetaIT,
  title={S100B(betabeta) inhibits the protein kinase C-dependent phosphorylation of a peptide derived from p53 in a Ca2+-dependent manner.},
  author={Paul T. Wilder and Richard R Rustandi and Alexander C. Drohat and David J. Weber},
  journal={Protein science : a publication of the Protein Society},
  year={1998},
  volume={7 3},
  pages={794-8}
}
S100B(betabeta) is a dimeric Ca2+-binding protein that is known to inhibit the protein kinase C (PKC)-dependent phosphorylation of several proteins. To further characterize this inhibition, we synthesized peptides based on the PKC phosphorylation domains of p53 (residues 367-388), neuromodulin (residues 37-53), and the regulatory domain of PKC (residues 19-31), and tested them as substrates for PKC. All three peptides were shown to be good substrates for the catalytic domain of PKC. As for full… CONTINUE READING

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