id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-343850-p4bbb6vm	Lin, Meng-Hsuan	Structural, Biophysical, and Biochemical Elucidation of the SARS-CoV-2 Nonstructural Protein 3 Macro Domain	2020-09-18		.txt	text/plain	5149	313	59	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. Virus macro domains were reported to have multiple functions, including a ADP-ribose (ADPR) 8−10 or poly-ADPR 9 interaction, adenine-rich RNA 11 binding, enzyme activities of ADPR-1″ phosphohydrolase, 7, 9 and the removal of mono(ADP-ribose) from protein.	./cache/cord-343850-p4bbb6vm.txt	./txt/cord-343850-p4bbb6vm.txt