Published in

American Society for Microbiology, Journal of Virology, 13(80), p. 6686-6690, 2006

DOI: 10.1128/jvi.02215-05

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Structure-Based Mutational Analysis of the NS3 Helicase from Dengue Virus

Journal article published in 2006 by Aruna Sampath, Ting Xu, Alex Chao, Dahai Luo ORCID, Julien Lescar, Subhash G. Vasudevan
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

ABSTRACT 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.