Structure-based mutational analysis of the NS3 helicase from dengue virus.
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ABSTRACT:
SUBMITTER: Sampath A
PROVIDER: S-EPMC1488930 | biostudies-literature | 2006 Jul
REPOSITORIES: biostudies-literature
Publications
Structure-based mutational analysis of the NS3 helicase from dengue virus.
Sampath Aruna A Xu Ting T Chao Alex A Luo Dahai D Lescar Julien J Vasudevan Subhash G SG
Journal of virology 20060701 13
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 ...[more]
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