Structural basis for unique mechanisms of folding and hemoglobin binding by a malarial protease.

@article{Wang2006StructuralBF,
  title={Structural basis for unique mechanisms of folding and hemoglobin binding by a malarial protease.},
  author={Stephanie X Wang and Kailash Chand Pandey and John R. Somoza and Puran Singh Sijwali and Tanja Kortemme and Linda S. Brinen and Robert Fletterick and Philip J. Rosenthal and James H McKerrow},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2006},
  volume={103 31},
  pages={11503-8}
}
Falcipain-2 (FP2), the major cysteine protease of the human malaria parasite Plasmodium falciparum, is a hemoglobinase and promising drug target. Here we report the crystal structure of FP2 in complex with a protease inhibitor, cystatin. The FP2 structure reveals two previously undescribed cysteine protease structural motifs, designated FP2(nose) and FP2(arm), in addition to details of the active site that will help focus inhibitor design. Unlike most cysteine proteases, FP2 does not require a… CONTINUE READING