These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Structure-based mutational analysis of the NS3 helicase from dengue virus.
    Author: Sampath A, Xu T, Chao A, Luo D, Lescar J, Vasudevan SG.
    Journal: J Virol; 2006 Jul; 80(13):6686-90. PubMed ID: 16775356.
    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.
    [Abstract] [Full Text] [Related] [New Search]