Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities.

@article{Watanabe2003AminoAS,
  title={Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities.},
  author={Leandra Watanabe and John D Shannon and Richard Hemmi Valente and Alexandra Rucavado and Alberto Alape-Gir{\'o}n and Aura S. Kamiguti and Robert David Geoffrey Theakston and J. Wesley Fox and Jos{\'e} Mar{\'i}a Guti{\'e}rrez and Raghuvir Krishnaswamy Arni},
  journal={Protein science : a publication of the Protein Society},
  year={2003},
  volume={12 10},
  pages={2273-81}
}
BaP1 is a 22.7-kD P-I-type zinc-dependent metalloproteinase isolated from the venom of the snake Bothrops asper, a medically relevant species in Central America. This enzyme exerts multiple tissue-damaging activities, including hemorrhage, myonecrosis, dermonecrosis, blistering, and edema. BaP1 is a single chain of 202 amino acids that shows highest sequence identity with metalloproteinases isolated from the venoms of snakes of the subfamily Crotalinae. It has six Cys residues involved in three… CONTINUE READING

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