id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-272710-uq2idlca	Cho, Chao-Cheng	Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module: CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES	2016-01-05		.txt	text/plain	4121	216	55	title: Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module: CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES The newly emerging Middle East respiratory syndrome coronavirus (MERS-CoV) encodes the conserved macro domain within non-structural protein 3. This study provides structural and biophysical bases to further evaluate the role of the MERS-CoV macro domain in the host response via ADP-ribose binding but also as a potential target for drug design. Variations in strength of the hydrogen bond and orientation of the side chain in Asp residues may result in differential binding affinities of ADP-ribose observed in macro domains of MERS-CoV (K d 2.95 M), SARS-CoV (K d 24 M) (36), and HCoV-229E (K d 28.9 M) (41) . Structural analysis revealed that differences in the context of hydrogen bonds formed by the conserved Asp with ADPribose and residues in ␣1 helices in macro domains of MERS-CoV, SARS-CoV, and HCoV-229E may result in differential binding affinities for ADP-ribose.	./cache/cord-272710-uq2idlca.txt	./txt/cord-272710-uq2idlca.txt