id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-305589-ofpna4k1	Schubert, Katharina	SARS-CoV-2 Nsp1 binds ribosomal mRNA channel to inhibit translation	2020-07-07		.txt	text/plain	4090	229	55	By combining cryo-electron microscopy and biochemical experiments, we show that SARS-CoV-2 Nsp1 binds to the human 40S subunit in ribosomal complexes including the 43S pre-initiation complex. Based on these results we assembled in vitro a 40S-Nsp1 complex and determined its structure at 2.8 Å resolution using cryo-EM (Extended Data Fig. 2 ). As observed in the high-resolution structure of the 40S-Nsp1 complex, the C-terminal part of Nsp1 in the mRNA entrance channel (Fig. 1e ) folds into two helices that interact with h18 of the 18S rRNA as well as proteins uS3 in the head and uS5 and eS30 in the body, respectively ( Fig. 1f; Fig. 2a ). Our structural data suggest that SARS-CoV-2 Nsp1 inhibits translation by sterically occluding the entrance region of the mRNA channel and interfering with binding of cellular mRNAs (Fig. 4a,b) .	./cache/cord-305589-ofpna4k1.txt	./txt/cord-305589-ofpna4k1.txt