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Journal article

Crystal structures and fragment screening of SARS-CoV-2 NSP14 reveal details of exoribonuclease activation and mRNA capping and provide starting points for antiviral drug development

Abstract:

NSP14 is a dual function enzyme containing an N-terminal exonuclease domain (ExoN) and C-terminal Guanine-N7-methyltransferase (N7-MTase) domain. Both activities are essential for the viral life cycle and may be targeted for anti-viral therapeutics. NSP14 forms a complex with NSP10, and this interaction enhances the nuclease but not the methyltransferase activity. We have determined the structure of SARS-CoV-2 NSP14 in the absence of NSP10 to 1.7 Å resolution. Comparisons with NSP14/NSP10 com...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1093/nar/gkac1207

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
CM CMD
Role:
Author
ORCID:
0000-0001-5167-3203
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
CM CMD
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
CM CMD
Role:
Author
ORCID:
0000-0003-4488-0516
Publisher:
Oxford University Press
Series:
Structural Biology
Journal:
Nucleic Acids Research More from this journal
Volume:
51
Issue:
1
Pages:
475–487
Place of publication:
England
Publication date:
2022-12-22
Acceptance date:
2022-12-09
DOI:
EISSN:
1362-4962
ISSN:
0305-1048
Pmid:
36546776
Language:
English
Keywords:
Pubs id:
1317547
Local pid:
pubs:1317547
Deposit date:
2023-01-23

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