A theoretical approach towards the identification of cleavage-determining amino acid motifs of the 20 S proteasome.

@article{Holzhtter1999ATA,
  title={A theoretical approach towards the identification of cleavage-determining amino acid motifs of the 20 S proteasome.},
  author={Hermann-Georg Holzh{\"u}tter and Cornelius Fr{\"o}mmel and Peter Michael Kloetzel},
  journal={Journal of molecular biology},
  year={1999},
  volume={286 4},
  pages={1251-65}
}
Hitherto the mechanisms controlling the selective cleavage of peptide bonds by the 20 S proteasome have been poorly understood. The observation that peptide bond cleavage may eventually occur at the carboxyl site of either amino acid residue rules out a simple control of cleavage preferences by the P1 residue alone. Here, we follow the rationale that the presence of specific cleavage-determining amino acids motifs (CDAAMs) around the scissile peptide bond are required for the attainment of… CONTINUE READING

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