id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-335955-2bw2sly8	Shi, Yuejun	A Dimerization-Dependent Mechanism Drives the Endoribonuclease Function of Porcine Reproductive and Respiratory Syndrome Virus nsp11	2016-04-14		.txt	text/plain	7045	383	53	The crystal structures of severe acute respiratory syndrome coronavirus (SARS-CoV) nsp15 and murine hepatitis virus (MHV) nsp15 show that the biological unit of nsp15 is a hexamer (19, 21) and that the N-terminal domain (NTD) is important for oligomerization (23) . We report the crystal structure of PRRSV endoribonuclease nsp11 and demonstrate that the folding of NendoU active site residues is widely conserved among members of the order Nidovirales (families Arteriviridae and Coronaviridae). Additionally, the structural comparison demonstrated that residues His129, His144, Lys173, Thr177, Asp180, Asp204, and Tyr219 from nsp11 superimpose well onto the corresponding residues of coronavirus nsp15 (Fig. 5 and 6 ), indicating the relative conservation of key active site residues and similar endoribonuclease cleavage mechanisms shared among nidoviruses (families Arteriviridae and Coronaviridae). In this study, endoribonuclease activity of the wild-type and mutant nsp11 protein was measured, and the results are shown in Fig. 7C .	./cache/cord-335955-2bw2sly8.txt	./txt/cord-335955-2bw2sly8.txt