What is it about?
Plasmepsin II, an aspartic protease from Plasmodium falciparum, the most letal parasite of malaria, has been co-crystallized with two inhibitors and their structure has been solved and studied, paying special attention to the interactions of the inhibitors with the active site of the enzyme, and compared with the structure of a another hydroxyethylamine-based inhibitor, previously studied.
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Why is it important?
Malaria is one of the most severe infectious diseases in the world. P. falciparum, the most lethal of the four parasites infecting humans, is becoming increasingly resistant to many of the current front- line antimalarial drugs, including chloroquine, quinine, arte- misinin and sulfadoxime/pyrimethamine. This highlights the urgent need for new efficacious drugs to combat this disease.
Perspectives
Solving the crystal structure of plasmepsin II with two inhibitors is a contribution to the structure-based drug design of new potent antimalarial inhibitors.
Dr Rosario Recacha
University of Oulu
Read the Original
This page is a summary of: Structures of plasmepsin II fromPlasmodium falciparumin complex with two hydroxyethylamine-based inhibitors, Acta Crystallographica Section F Structural Biology Communications, November 2015, International Union of Crystallography,
DOI: 10.1107/s2053230x15022049.
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