MedicGo
Crystal structure of the NS3 helicase of tick-borne encephalitis virus.
Metadata
Journalbiochemical and biophysical research communications2.985Date
2020 Jun 04
4 months ago
Type
Journal Article
Volume
2020-Jul-30 / 528 : 601-606
Author
Chen C 1, Han X 2, Chen C 3, Wang F 4, Huang J 5, Zhang L 6, Wang Z 7, Yang H 8
Affiliation
  • 2. School of Life Sciences, Tianjin University, Tianjin, China. Electronic address: [email protected]
  • 3. School of Life Sciences, Tianjin University, Tianjin, China; Tianjin International Joint Academy of Biotechnology and Medicine, Tianjin, China. Electronic address: [email protected]
  • 4. School of Life Sciences, Tianjin University, Tianjin, China. Electronic address: [email protected]
  • 5. School of Life Sciences, Tianjin University, Tianjin, China. Electronic address: [email protected]
  • 6. School of Life Sciences, Tianjin University, Tianjin, China. Electronic address: [email protected]
  • 7. School of Life Sciences, Tianjin University, Tianjin, China; Tianjin International Joint Academy of Biotechnology and Medicine, Tianjin, China. Electronic address: [email protected]
  • 8. School of Life Sciences, Tianjin University, Tianjin, China; Tianjin International Joint Academy of Biotechnology and Medicine, Tianjin, China. Electronic address: [email protected]
Doi
PMIDMESH
Abstract
Tick-borne encephalitis virus (TBEV) is a positive-sense single-stranded RNA virus belonging to the genus Flavivirus in Flaviviridae. It can cause the server infectious diseases named tick-borne encephalitis (TBE), which is characterized by paralysis and epilepsy. However, no effective treatment for TBE has been developed targeting TBEV. The NS3 helicase from TBEV plays an essential role in viral replication, which makes it an important target for drug design. In this study, the crystal structure of TBEV NS3 helicase has been determined to the resolution of 2.14 Å. Subsequent alignment with homologous structures reveals that the NTP binding site and RNA-binding sites are located in motifs Ⅱ and Ⅵ of NS3 and the critical residues for binding are conserved across species in the genus, while the distinct conformation transition implies that the TBEV helicase need a different local rearrangement. This study demonstrates the key atomic-level features of TBEV helicase and provides basis for the design of antiviral drugs targeting TBEV helicase.
Keywords: Crystal structure Helicase Tick-borne encephalitis Tick-borne encephalitis virus
Fav
Like
Download
Share
Export
Cite
3.0
Biochem Biophys Res Communbiochemical and biophysical research communications
Metadata
LocationUnited States
FromACADEMIC PRESS INC ELSEVIER SCIENCE

No Data

© 2017 - 2020 Medicgo
Powered by some medical students