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Structure of the yellow fever NS5 protein reveals conserved drug targets shared among flaviviruses

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F19%3A00517786" target="_blank" >RIV/61388963:_____/19:00517786 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.sciencedirect.com/science/article/abs/pii/S0166354219302116?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/abs/pii/S0166354219302116?via%3Dihub</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.antiviral.2019.104536" target="_blank" >10.1016/j.antiviral.2019.104536</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structure of the yellow fever NS5 protein reveals conserved drug targets shared among flaviviruses

  • Original language description

    Yellow fever virus (YFV) is responsible for devastating outbreaks of Yellow fever (YF) in humans and is associated with high mortality rates. Recent large epidemics and epizootics and exponential increases in the numbers of YF cases in humans and non-human primates highlight the increasing threat YFV poses, despite the availability of an effective YFV vaccine. YFV is the first human virus discovered, but the structures of several of the viral proteins remain poorly understood. Here we report the structure of the full-length NS5 protein, a key enzyme for the replication of flaviviruses that contains both a methyltransferase domain and an RNA dependent RNA polymerase domain, at 3.1 angstrom resolution. The viral polymerase adopts right-hand fold, demonstrating the similarities of the Yellow fever, Dengue and Zika polymerases. Together this data suggests NS5 as a prime and ideal target for the design of pan-flavivirus inhibitors.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/EF16_019%2F0000729" target="_blank" >EF16_019/0000729: Chemical biology for drugging undruggable targets</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2019

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Antiviral Research

  • ISSN

    0166-3542

  • e-ISSN

  • Volume of the periodical

    169

  • Issue of the periodical within the volume

    Sep

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    8

  • Pages from-to

    104536

  • UT code for WoS article

    000499934800002

  • EID of the result in the Scopus database

    2-s2.0-85067601232