A point mutation abolishes the helicase but not the nucleoside triphosphatase activity of hepatitis C virus NS3 protein.
The NS3 protein of hepatitis C virus contains a bipartite structure consisting of an N-terminal serine protease and a C-terminal DEAD box helicase. We show that the C-terminal domain has ATPase and panhelicase activities. The integrity of the helicase function is dependent on the conserved DEAD moti...
Furkejuvvon:
| Publikašuvnnas: | J Virol |
|---|---|
| Váldodahkkit: | , |
| Materiálatiipa: | Artigo |
| Giella: | Inglês |
| Almmustuhtton: |
American Society for Microbiology (ASM)
1997
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| Fáttát: | |
| Liŋkkat: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC191896/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9223530/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.71.8.6264-6266.1997 |
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