2'-O methylation of RNA cap in SARS-CoV-2 captured by serial crystallography.
Proc Natl Acad Sci U S A
; 118(21)2021 05 25.
Article
in English
| MEDLINE | ID: covidwho-1223143
Preprint
This scientific journal article is probably based on a previously available preprint. It has been identified through a machine matching algorithm, human confirmation is still pending.
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This scientific journal article is probably based on a previously available preprint. It has been identified through a machine matching algorithm, human confirmation is still pending.
See preprint
ABSTRACT
The genome of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) coronavirus has a capping modification at the 5'-untranslated region (UTR) to prevent its degradation by host nucleases. These modifications are performed by the Nsp10/14 and Nsp10/16 heterodimers using S-adenosylmethionine as the methyl donor. Nsp10/16 heterodimer is responsible for the methylation at the ribose 2'-O position of the first nucleotide. To investigate the conformational changes of the complex during 2'-O methyltransferase activity, we used a fixed-target serial synchrotron crystallography method at room temperature. We determined crystal structures of Nsp10/16 with substrates and products that revealed the states before and after methylation, occurring within the crystals during the experiments. Here we report the crystal structure of Nsp10/16 in complex with Cap-1 analog (m7GpppAm2'-O). Inhibition of Nsp16 activity may reduce viral proliferation, making this protein an attractive drug target.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
RNA Caps
/
RNA, Messenger
/
RNA, Viral
/
SARS-CoV-2
Type of study:
Experimental Studies
Language:
English
Year:
2021
Document Type:
Article
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