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• W2909804983 abstract "Falcipain-2 (FP2) and falcipain-3 (FP3) constitute the major hemoglobinases of Plasmodium falciparum. Previous biochemical and structural studies have explained the mechanism of inhibition of these enzymes by small molecules. However, a residue-level protein-protein interaction (PPI) with its natural macromolecular substrate, hemoglobin is not fully characterized. Earlier studies have identified a short motif in the C-terminal of FP2, an exosite protruding away from the active site, essential for hemoglobin degradation. Our structural and mutagenesis studies suggest that hemoglobin interacts with FP2 via specific interactions mediated by Glu185 and Val187 within the C-terminal motif, which are essential for hemoglobin binding. Since FP3 is also a major hemoglobinase and essential for parasite survival, we further demonstrate its interactions with hemoglobin. Our results suggest that Asp194 of FP3 is required for hemoglobin hydrolysis and residue-swap experiments confirmed that this position is functionally conserved between the two hemoglobinases. Residues involved in protein–protein interactions constitute important targets for drug-mediated inhibition. Targeting protein–protein interactions at exosites may likely be less susceptible to emergence of drug resistance and thus is a new field to explore in malaria." @default.
• W2909804983 created "2019-01-25" @default.
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• W2909804983 date "2019-02-01" @default.
• W2909804983 modified "2023-10-14" @default.
• W2909804983 title "Crucial residues in falcipains that mediate hemoglobin hydrolysis" @default.
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• W2909804983 doi "https://doi.org/10.1016/j.exppara.2019.01.005" @default.
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