Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications.

@article{Luo2010FlexibilityBT,
  title={Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications.},
  author={Dahai Luo and Na Wei and Danny N. Doan and Prasad N Paradkar and Yuwen Chong and Andrew D. Davidson and Masayo Kotaka and Julien Lescar and Subhash G. Vasudevan},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 24},
  pages={
          18817-27
        }
}
The dengue virus (DENV) NS3 protein is essential for viral polyprotein processing and RNA replication. It contains an N-terminal serine protease region (residues 1-168) joined to an RNA helicase (residues 180-618) by an 11-amino acid linker (169-179). The structure at 3.15 A of the soluble NS3 protein from DENV4 covalently attached to 18 residues of the NS2B cofactor region (NS2B(18)NS3) revealed an elongated molecule with the protease domain abutting subdomains I and II of the helicase (Luo, D… CONTINUE READING

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