| Literature DB >> 16775356 |
Aruna Sampath1, Ting Xu, Alex Chao, Dahai Luo, Julien Lescar, Subhash G Vasudevan.
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.Entities:
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Year: 2006 PMID: 16775356 PMCID: PMC1488930 DOI: 10.1128/JVI.02215-05
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103