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Journal of Tropical Medicine
Volume 2012, Article ID 345195, 11 pages
Review Article

Structure-Function of Falcipains: Malarial Cysteine Proteases

Host-Parasite Interaction Biology Group, National Institute of Malaria Research, Indian Council of Medical Research, Sector-8, Dwarka, New Delhi 110 077, India

Received 6 July 2011; Revised 12 October 2011; Accepted 27 October 2011

Academic Editor: M. C. Field

Copyright © 2011 Kailash C. Pandey and Rajnikant Dixit. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Evidence indicates that cysteine proteases play essential role in malaria parasites; therefore an obvious area of investigation is the inhibition of these enzymes to treat malaria. Studies with cysteine protease inhibitors and manipulating cysteine proteases genes have suggested a role for cysteine proteases in hemoglobin hydrolysis. The best characterized Plasmodium cysteine proteases are falcipains, which are papain family enzymes. Falcipain-2 and falcipain-3 are major hemoglobinases of P. falciparum. Structural and functional analysis of falcipains showed that they have unique domains including a refolding domain and a hemoglobin binding domain. Overall, the complexes of falcipain-2 and falcipain-3 with small and macromolecular inhibitors provide structural insight to facilitate the design or modification of effective drug treatment against malaria. Drug development targeting falcipains should be aided by a strong foundation of biochemical and structural studies.