id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-333099-hy4nmy7l	Thoms, Matthias	Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2	2020-07-17		.txt	text/plain	3441	219	53	Here, we show that Nsp1 from SARS-CoV-2 binds to the 40S ribosomal subunit, resulting in shutdown of mRNA translation both in vitro and in cells. To elucidate the molecular interaction of SARS-CoV-2 Nsp1 with human ribosomes, we reconstituted a complex from purified, recombinant Nsp1 and purified human 40S ribosomal subunits and determined its structure by cryo-EM at an average resolution of 2.6 Å (Fig. 2, A and B , and figs. To characterize the ribosomal targets and the mode of interaction of Nsp1 in human cells, we expressed N-terminally 3xFLAG tagged Nsp1 in HEK293T cells and affinity purified associated native complexes for analysis by cryo-EM and mass spectrometry (Fig. 2E , figs. The second major population of Nsp1-bound 80S ribosomes (Fig. 2 , M and N) lacked CCDC124, but contained the cell growth regulating nucleolar protein LYAR, which has been implicated in processing of pre-rRNA and in negative regulation of antiviral innate immune responses (34, 35) .	./cache/cord-333099-hy4nmy7l.txt	./txt/cord-333099-hy4nmy7l.txt