Structural analysis of the SARS-CoV-2 methyltransferase complex involved in RNA cap creation bound to sinefungin

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A90127%2F20%3A00139241" target="_blank" >RIV/00216224:90127/20:00139241 - isvavai.cz</a>

Alternative codes found

RIV/61388963:_____/20:00531271

Result on the web

<a href="https://www.nature.com/articles/s41467-020-17495-9" target="_blank" >https://www.nature.com/articles/s41467-020-17495-9</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41467-020-17495-9" target="_blank" >10.1038/s41467-020-17495-9</a>

Result language

angličtina

Original language name

Structural analysis of the SARS-CoV-2 methyltransferase complex involved in RNA cap creation bound to sinefungin

Original language description

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the cause of the COVID-19 pandemic. 2-O-RNA methyltransferase (MTase) is one of the enzymes of this virus that is a potential target for antiviral therapy as it is crucial for RNA cap formation; an essential process for viral RNA stability. This MTase function is associated with the nsp16 protein, which requires a cofactor, nsp10, for its proper activity. Here we show the crystal structure of the nsp10-nsp16 complex bound to the pan-MTase inhibitor sinefungin in the active site. Our structural comparisons reveal low conservation of the MTase catalytic site between Zika and SARS-CoV-2 viruses, but high conservation of the MTase active site between SARS-CoV-2 and SARS-CoV viruses; these data suggest that the preparation of MTase inhibitors targeting several coronaviruses - but not flaviviruses - should be feasible. Together, our data add to important information for structure-based drug discovery. p id=Par SARS-CoV-2 expresses a 2 ' -O RNA methyltransferase (MTase) that is involved in the viral RNA cap formation and therefore a target for antiviral therapy. Here the authors provide the structure of nsp10-nsp16 with the panMTase inhibitor sinefungin and report that the development of MTase inhibitor therapies that target multiple coronoaviruses is feasible.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

30300 - Health sciences

Project

—

Continuities

—

Publication year

2020

Confidentiality

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

Name of the periodical

Nature Communications

ISSN

2041-1723

e-ISSN

—

Volume of the periodical

11

Issue of the periodical within the volume

1

Country of publishing house

DE - GERMANY

Number of pages

7

Pages from-to

1-7

UT code for WoS article

000556360300010

EID of the result in the Scopus database

2-s2.0-85090483661