Favourable side-chain orientation of cleavage site dibasic residues of prohormone in proteolytic processing by prohormone convertase 1/3.

@article{Brakch2000FavourableSO,
  title={Favourable side-chain orientation of cleavage site dibasic residues of prohormone in proteolytic processing by prohormone convertase 1/3.},
  author={N. Brakch and M. Rholam and M. Simonetti and P. Cohen},
  journal={European journal of biochemistry},
  year={2000},
  volume={267 6},
  pages={
          1626-33
        }
}
  • N. Brakch, M. Rholam, +1 author P. Cohen
  • Published 2000
  • Medicine, Chemistry
  • European journal of biochemistry
  • Previous studies using selectively modified pro-ocytocin/neurophysin substrate analogues and the purified metalloprotease, pro-ocytocin/neurophysin convertase (magnolysin; EC 3.4 24.62), have shown that dibasic cleavage site processing is associated with a prohormone sequence organized in a beta-turn structure. We have used various peptide analogues of the pro-ocytocin-neurophysin processing domain, and recombinant prohormone convertase 1/3, to test the validity of this property towards this… CONTINUE READING
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