id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-262318-qpztmdnw	Guo, Jingxu	In crystallo-screening for discovery of human norovirus 3C-like protease inhibitors	2020-07-16		.txt	text/plain	6348	319	58	In this work we have crystallised the protease in its native form with an unperturbed catalytic triad and have conducted crystal-based fragment screening of 844 compounds with the aim of discovering novel inhibitory functional groups which have the potential to be developed as therapeutic agents, either on their own or through chemical coupling. Interestingly, the β-hairpin formed by β9 and β10, which is involved in binding the N-terminal side of the substrate peptide, adopts an appreciably different conformation from that observed in an earlier inhibitor-complexed structure ( The SV3CP enzyme has approximately 90 % sequence identity with other GI noroviral 3C proteases and an identity of the order of 68 % with the enzyme from the GII genotype. The X-ray structure of the Southampton virus 3CL pro has been determined at 1.3 Å resolution in a crystal form that has allowed fragment-screening for novel inhibitors to be undertaken at similar resolutions.	./cache/cord-262318-qpztmdnw.txt	./txt/cord-262318-qpztmdnw.txt