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Plasmodium falciparum is the parasite responsible
for more than 90% of deaths caused by the global
epidemic of malaria.The enzyme thymidylate synthase-
dihydrofolate reductase (TS-DHFR) is a major
antimalarial drug target, and mutations in this
enzyme have caused widespread resistance.Our work
comprises the first systematic, mechanistic
characterization of TS-DHFR and its non-active
site regions.Our kinetic data show this
bifunctional enzyme is regulated by elegant
interdomain communication, as well as catalytic
contributions from distant structural regions, far
from the active sites. Understanding the role of
these unique regions may lead to more specific, less
toxic therapies.Also, molecular docking and virtual
screening of this enzyme identified a lead compound
which inhibits both wildtype and drug-resistant
parasites.Co-crystal structures of enzyme with
compound suggest a molecular basis for overcoming
drug resistance.This work demonstrates how in-depth
kinetic analyses can be used to identify novel
intramolecular targets for rational drug design, and
should be useful specially to students of
enzymology, protein biochemistry and
pharmacology.
for more than 90% of deaths caused by the global
epidemic of malaria.The enzyme thymidylate synthase-
dihydrofolate reductase (TS-DHFR) is a major
antimalarial drug target, and mutations in this
enzyme have caused widespread resistance.Our work
comprises the first systematic, mechanistic
characterization of TS-DHFR and its non-active
site regions.Our kinetic data show this
bifunctional enzyme is regulated by elegant
interdomain communication, as well as catalytic
contributions from distant structural regions, far
from the active sites. Understanding the role of
these unique regions may lead to more specific, less
toxic therapies.Also, molecular docking and virtual
screening of this enzyme identified a lead compound
which inhibits both wildtype and drug-resistant
parasites.Co-crystal structures of enzyme with
compound suggest a molecular basis for overcoming
drug resistance.This work demonstrates how in-depth
kinetic analyses can be used to identify novel
intramolecular targets for rational drug design, and
should be useful specially to students of
enzymology, protein biochemistry and
pharmacology.