An evolutionarily conserved tripartite tryptophan motif stabilizes the prodomains of cathepsin L-like cysteine proteases.

@article{Kreusch2000AnEC,
  title={An evolutionarily conserved tripartite tryptophan motif stabilizes the prodomains of cathepsin L-like cysteine proteases.},
  author={Stefan Kreusch and Marc Fehn and Gunter Maubach and Karl Nissler and Winfried Rommerskirch and K. Schilling and Ekkehard Weber and Ingrid Wenz and Bernd Wiederanders},
  journal={European journal of biochemistry},
  year={2000},
  volume={267 10},
  pages={2965-72}
}
Cathepsin L-like cysteine proteinases contain an evolutionarily highly conserved alpha-helical motif in the proregion. This is called the ER(F/W)N(I/V)N motif according to the conserved amino acids along one side of the helix. We studied the function of this motif using site-directed mutagenesis experiments of human procathepsin S. We replaced each of these amino acids with alanine and constructed deletion mutants lacking parts of the helix. All mutants were expressed in HEK 293 cells, but only… CONTINUE READING

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