Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from Plasmodium falciparum

@article{Bernstein1999CrystalSO,
  title={Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from Plasmodium falciparum},
  author={Nina Khazanovich Bernstein and Maia M. Cherney and Hansruedi Loetscher and Robert G. Ridley and Michael N. G. James},
  journal={Nature Structural Biology},
  year={1999},
  volume={6},
  pages={32-37}
}
Proplasmepsin II is the zymogen of plasmepsin II, an aspartic proteinase used by Plasmodium falciparum to digest hemoglobin during the blood stage of malaria. A large shift between the N–domain and the central and C–domains of proplasmepsin II opens the active site cleft, preventing the formation of a functional aspartic proteinase active site. This mode of inhibition of catalytic activity has not been observed in any other aspartic proteinase zymogen. Instead of occluding a pre–formed active… CONTINUE READING