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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

期刊

BIOMOLECULAR NMR ASSIGNMENTS
卷 16, 期 1, 页码 9-16

出版社

SPRINGER
DOI: 10.1007/s12104-021-10052-5

关键词

SARS-CoV; MERS-CoV; Non-structural protein; Solution NMR-spectroscopy; Macro domains; NMR backbone assignment

资金

  1. General Secretariat for Research and Technology & EU - NSRF 2014-2020 [INSPIRED MIS 5002550]
  2. FP7 Research Potential of Convergence Regions [EU FP7 REGPOT CT-2011-285950]

向作者/读者索取更多资源

The Macro Domains (MDs) of SARS-CoV and MERS-CoV exhibit topological and conformational features similar to the nsP3b macro domain of SARS-CoV-2, making them important drug targets for potential antiviral drugs.
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 alpha/beta/alpha 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 (H-1, C-13, N-15) 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.

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