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• W2063808230 endingPage "6159" @default.
• W2063808230 startingPage "6151" @default.
• W2063808230 abstract "Aurintricarboxylic acid (ATA) is a potent inhibitor of many enzymes needed for cell and virus replication, such as polymerases, helicases, nucleases, and topoisomerases. This study examines how ATA interacts with the helicase encoded by the hepatitis C virus (HCV) and reveals that ATA interferes with both nucleic acid and ATP binding to the enzyme. We show that ATA directly binds HCV helicase to prevent the enzyme from interacting with nucleic acids and to modulate the affinity of HCV helicase for ATP, the fuel for helicase action. Amino acid substitutions in the helicase DNA binding cleft or its ATP binding site alter the ability of ATA to disrupt helicase-DNA interactions. These data, along with molecular modeling results, support the notion that an ATA polymer binds between Arg467 and Glu493 to prevent the helicase from binding either ATP or nucleic acids. We also characterize how ATA affects the kinetics of helicase-catalyzed ATP hydrolysis, and thermodynamic parameters describing the direct interaction between HCV helicase and ATA using microcalorimetry. The thermodynamics of ATA binding to HCV helicase reveal that ATA binding does not mimic nucleic acid binding in that ATA binding is driven by a smaller enthalpy change and an increase in entropy." @default.
• W2063808230 created "2016-06-24" @default.
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• W2063808230 date "2013-08-26" @default.
• W2063808230 modified "2023-10-16" @default.
• W2063808230 title "Aurintricarboxylic Acid Modulates the Affinity of Hepatitis C Virus NS3 Helicase for Both Nucleic Acid and ATP" @default.
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• W2063808230 doi "https://doi.org/10.1021/bi4006495" @default.
• W2063808230 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4272346" @default.
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• W2063808230 hasPublicationYear "2013" @default.
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