期刊
JOURNAL OF VIROLOGY
卷 80, 期 13, 页码 6686-6690出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.02215-05
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We performed a mutational analysis of the NS3 helicase of dengue virus to test insights gleaned from its crystal structure and identified four residues in the full-length protein that severely impaired either its RTPase and ATPase (Arg-457-458, Arg-460, Arg-463) or helicase (Ile-365, Arg-376) activity. Alanine substitution of Lys-396, which is located at the surface of domain II, drastically reduced all three enzymatic activities. Our study points to a pocket at the surface of domain II that may be suitable for the design of allosteric inhibitors.
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