Dataset Information


Structural, Biophysical, and Biochemical Elucidation of the SARS-CoV-2 Nonstructural Protein 3 Macro Domain.

ABSTRACT: The pandemic outbreak of a novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has threatened the global public health and economy since late December 2019. SARS-CoV-2 encodes the conserved macro domain within nonstructural protein 3, which may reverse cellular ADP-ribosylation and potentially cut the signal of a viral infection in the cell. Herein, we report that the SARS-CoV-2 macro domain was examined as a poly-ADP-ribose (ADPR) binding module and possessed mono-ADPR cleavage enzyme activity. After confirming the ADPR binding ability via a biophysical approach, the X-ray crystal structure of the SARS-CoV-2 macro domain was determined and structurally compared with those of other viruses. This study provides structural, biophysical, and biochemical bases to further evaluate the role of the SARS-CoV-2 macro domain in the host response via ADP-ribose binding but also as a potential target for drug design against COVID-19.


PROVIDER: S-EPMC7537548 | BioStudies | 2020-01-01

REPOSITORIES: biostudies

Similar Datasets

2021-01-01 | S-EPMC7840908 | BioStudies
2016-01-01 | S-EPMC4777827 | BioStudies
2006-01-01 | S-EPMC1563857 | BioStudies
2020-01-01 | S-EPMC7468284 | BioStudies
2006-01-01 | S-EPMC2222557 | BioStudies
2019-01-01 | S-EPMC7111667 | BioStudies
2021-01-01 | S-EPMC7826497 | BioStudies
2020-01-01 | S-EPMC7566600 | BioStudies
2009-01-01 | S-EPMC7094737 | BioStudies
2015-01-01 | S-EPMC4567502 | BioStudies