NMR study of macro domains (MDs) from betacoronavirus: backbone resonance assignments of SARS-CoV and MERS-CoV MDs in the free and the ADPr-bound state.
Biomol NMR Assign
; 16(1): 9-16, 2022 04.
Article
in English
| MEDLINE | ID: covidwho-1482296
ABSTRACT
SARS-CoV and MERS-CoV Macro Domains (MDs) exhibit topological and conformational features that resemble the nsP3b macro (or "X") domain of SARS-CoV-2. Indeed, all the three domains (SARS-CoV-2, SARS-CoV and MERS-CoV MDs) fold in a three-layer α/ß/α sandwich structure, as reported by crystallographic structural investigation of SARS-CoV MD and MERS-CoV MD. These viral MDs are able to bind ADP-ribose as many other MDs from different kingdoms. They have been characterized also as de-ADP-ribosylating enzymes. For this reason, these viral macrodomains recently emerged as important drug targets since they can counteract antiviral ADP-ribosylation mediated by poly-ADP-ribose polymerase (PARPs). Even in presence of the 3D structures of SARS-CoV MD and of MERS-CoV MD, we report herein the almost complete NMR backbone (1H, 13C, 15N) of SARS-CoV MD and MERS-CoV proteins in the free and ADPr bound forms, and the NMR chemical shift-based prediction of their secondary structure elements. These NMR data will help to further understanding of the atomic-level conformational dynamics of these proteins and will allow an extensive screening of small molecules as potential antiviral drugs.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Middle East Respiratory Syndrome Coronavirus
/
COVID-19
Type of study:
Prognostic study
Limits:
Humans
Language:
English
Journal:
Biomol NMR Assign
Journal subject:
Molecular Biology
/
Nuclear Medicine
Year:
2022
Document Type:
Article
Affiliation country:
S12104-021-10052-5
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