id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-335308-5kh7wgvx	Ponnusamy, Rajesh	Variable Oligomerization Modes in Coronavirus Non-structural Protein 9	2008-11-28		.txt	text/plain	10725	580	62	In the crystal, the wild-type HCoV-229E protein forms a trimer of dimers, whereas the mutant and SARS-CoV Nsp9 are organized in rod-like polymers. Although the residue responsible for disulfide formation in HCoV-229E Nsp9, Cys69, is conserved in SARS-CoV Nsp9, and the sequence identity is as high as 45% between the two proteins (see Supplementary Data Fig. S3 ), the mode of dimerization in the latter is very different from what we observe in our structure. Wild-type SARS-CoV Nsp9 and the HCoV-229E Nsp9 Cys69Ala mutant form higher oligomers at a protein concentration of 100 μM, presumably involving interactions similar to those seen in the crystal structure. On the other hand, the HCoV-229E Cys69Ala mutant has a dimerization mode similar to that of the wild-type SARS-CoV Nsp9 but it does not show binding with the nucleic acid in the gel mobility-shift experiment (except for the small shift seen for the 55-mer, the longest oligonucleotide tested).	./cache/cord-335308-5kh7wgvx.txt	./txt/cord-335308-5kh7wgvx.txt