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Structure-Function of Falcipains: Malarial Cysteine Proteases

Authors
Journal
Journal of Tropical Medicine
1687-9686
Publisher
Hindawi Publishing Corporation
Publication Date
Volume
2012
Identifiers
DOI: 10.1155/2012/345195
Keywords
  • Review Article
Disciplines
  • Biology
  • Chemistry
  • Design
  • Medicine

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.

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