The structure of Zika virus NS5 reveals a conserved domain conformation
| Autor: | Stephanie Thurmond, Boxiao Wang, Xiao-Feng Tan, Zhi-Min Zhang, Rong Hai, Jikui Song, Asher Lin |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Protein Conformation viruses General Physics and Astronomy Viral Nonstructural Proteins medicine.disease_cause Crystallography X-Ray Zika virus chemistry.chemical_compound Protein structure RNA polymerase Viral Conserved Sequence Subgenomic mRNA Multidisciplinary Crystallography biology virus diseases 3. Good health Flavivirus RNA Replicase Infectious Diseases Templates Generic Health Relevance RNA Viral Infection Viral protein Science 030106 microbiology Protein domain RNA-dependent RNA polymerase Antiviral Agents General Biochemistry Genetics and Molecular Biology Article 03 medical and health sciences Genetic medicine Genetics Amino Acid Sequence Binding Sites Prevention General Chemistry Templates Genetic Zika Virus biology.organism_classification RNA-Dependent RNA Polymerase Virology 030104 developmental biology Good Health and Well Being Emerging Infectious Diseases chemistry X-Ray RNA |
| Zdroj: | Nature communications, vol 8, iss 1 Nature Communications Nature Communications, Vol 8, Iss 1, Pp 1-6 (2017) Wang, B; Tan, X-F; Thurmond, S; Zhang, Z-M; Lin, A; Hai, R; et al.(2017). The structure of Zika virus NS5 reveals a conserved domain conformation. NATURE COMMUNICATIONS, 8. doi: 10.1038/ncomms14763. UC Riverside: Retrieved from: http://www.escholarship.org/uc/item/3217r5rw |
| DOI: | 10.1038/ncomms14763. |
| Popis: | The recent outbreak of Zika virus (ZIKV) has imposed a serious threat to public health. Here we report the crystal structure of the ZIKV NS5 protein in complex with S-adenosyl-L-homocysteine, in which the tandem methyltransferase (MTase) and RNA-dependent RNA polymerase (RdRp) domains stack into one of the two alternative conformations of flavivirus NS5 proteins. The activity of this NS5 protein is verified through a de novo RdRp assay on a subgenomic ZIKV RNA template. Importantly, our structural analysis leads to the identification of a potential drug-binding site of ZIKV NS5, which might facilitate the development of novel antivirals for ZIKV. The recent outbreak of Zika virus is a major worldwide health concern and effective drugs are currently not available. Here the authors present the structure of Zika non-structural protein 5 and identify a potential drug-binding site, which might facilitate the development of novel antivirals. |
| Databáze: | OpenAIRE |
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