Novel uncomplexed and complexed structures of plasmepsin II, an aspartic protease from Plasmodium falciparum.

@article{Asojo2003NovelUA,
  title={Novel uncomplexed and complexed structures of plasmepsin II, an aspartic protease from Plasmodium falciparum.},
  author={O. Asojo and S. Gulnik and E. Afonina and Betty Yu and J. Ellman and T. Haque and Abelardo M Silva},
  journal={Journal of molecular biology},
  year={2003},
  volume={327 1},
  pages={
          173-81
        }
}
Malaria remains a human disease of global significance and a major cause of high infant mortality in endemic nations. Parasites of the genus Plasmodium cause the disease by degrading human hemoglobin as a source of amino acids for their growth and maturation. Hemoglobin degradation is initiated by aspartic proteases, termed plasmepsins, with a cleavage at the alpha-chain between residues Phe33 and Leu34. Plasmepsin II is one of the four catalytically active plasmepsins that has been identified… Expand
Inhibitor binding to the plasmepsin IV aspartic protease from Plasmodium falciparum.
Structure of the aspartic protease plasmepsin 4 from the malarial parasite Plasmodium malariae bound to an allophenylnorstatine-based inhibitor.
X-ray Structure of Plasmepsin II Complexed with a Potent Achiral Inhibitor*
Structures of plasmepsin II from Plasmodium falciparum in complex with two hydroxyethylamine-based inhibitors.
Crystal structures of the free and inhibited forms of plasmepsin I (PMI) from Plasmodium falciparum.
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