Abstract
Helicases form an attractive protein family for drug discovery because they are involved in various human diseases. In this report, we show that it is possible to inhibit both the ATPase and the helicase activities of a DNA helicase with dibenzothiepins that bind at its nucleic acid binding site. These results suggest a drug discovery strategy to inhibit DNA helicases.
MeSH terms
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Adenosine Triphosphatases / antagonists & inhibitors
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Binding Sites
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Binding, Competitive / drug effects
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Crystallography, X-Ray
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DNA / chemistry
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DNA / drug effects*
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DNA Helicases / antagonists & inhibitors*
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Dibenzothiepins / chemistry
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Dibenzothiepins / pharmacology*
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Escherichia coli / enzymology
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Escherichia coli Proteins / antagonists & inhibitors*
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Models, Molecular
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Molecular Structure
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Protein Conformation
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Protein Structure, Tertiary
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Structure-Activity Relationship
Substances
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Dibenzothiepins
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Enzyme Inhibitors
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Escherichia coli Proteins
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DNA
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Adenosine Triphosphatases
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helD protein, E coli
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DNA Helicases