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Journal of Virology, July 2006, p. 6686-6690, Vol. 80, No. 13
0022-538X/06/$08.00+0     doi:10.1128/JVI.02215-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

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

Aruna Sampath,1,{dagger} Ting Xu,2,{dagger} Alex Chao,1 Dahai Luo,2 Julien Lescar,2* and Subhash G. Vasudevan1*

Novartis Institute for Tropical Diseases, 10 Biopolis Road, Chromos Building, Singapore 138670, Singapore,1 School of Biological Sciences, Nanyang Technological University, 60, Nanyang Drive, Singapore 637551, Singapore2

Received 20 October 2005/ Accepted 10 April 2006

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.


* Corresponding author. Mailing address for Julien Lescar: School of Biological Sciences, Nanyang Technological University, 60, Nanyang Drive, Singapore 637551, Singapore. E-mail: julien{at}ntu.edu.sg. Mailing address for Subhash Vasudevan: Novartis Institute for Tropical Diseases, 10 Biopolis Road, Chromos Building, Singapore 138670, Singapore. Phone: 65 67222909. Fax: 011-65-67222916. E-mail: subhash.vasudevan{at}novartis.com.

{dagger} These two authors contributed equally to this work.


Journal of Virology, July 2006, p. 6686-6690, Vol. 80, No. 13
0022-538X/06/$08.00+0     doi:10.1128/JVI.02215-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.




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