title: Structure-function of falcipains: malarial cysteine proteases.
abstract: 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.
authors.affiliation: Host-Parasite Interaction Biology Group, National Institute of Malaria Research, Indian Council of Medical Research, Sector-8, Dwarka, New Delhi 110 077, India.
authors.forename: Kailash C
authors.initials: KC
authors.lastname: Pandey
authors.forename: Rajnikant
authors.initials: R
authors.lastname: Dixit