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. 2019 Mar 5;10:394. doi: 10.3389/fmicb.2019.00394

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Copyright © 2019 Mishra, Singh and Singh.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Overall structure of Falcipains. Cartoon representation of Falcipain-2 (PDB: 2GHU) displaying two distinct domains and a prominent active site cleft. Active site residues Cys-42 (Red), His-174 (Gray), and Asn-204 (Magenta) are shown as spheres. Papain (PDB: 9PAP; shown in yellow) as a model papain-like cysteine protease is superimposed. N-terminal extension (shown in blue) and the hemoglobin binding hairpin (HBH- shown in orange) are specific to plasmodial falcipains and not observed in other papain-like cysteine proteases. A detailed view of side chains of residues in the HBH are shown in the inset. All structure figures have been made in Pymol.