id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-286537-7ri2p5b8	Lee, Ting-Wai	Crystal Structures of the Main Peptidase from the SARS Coronavirus Inhibited by a Substrate-like Aza-peptide Epoxide	2005-11-11		.txt	text/plain	7020	365	61	authors: Lee, Ting-Wai; Cherney, Maia M.; Huitema, Carly; Liu, Jie; James, Karen Ellis; Powers, James C.; Eltis, Lindsay D.; James, Michael N.G. title: Crystal Structures of the Main Peptidase from the SARS Coronavirus Inhibited by a Substrate-like Aza-peptide Epoxide The crystal structures of the Mpro:APE complex in the space groups C2 and P212121 revealed the formation of a covalent bond between the catalytic Cys145 Sγ atom of the peptidase and the epoxide C3 atom of the inhibitor, substantiating the mode of action of this class of cysteine-peptidase inhibitors. In contrast, in protomer A of the M pro CAðK1Þ :APE complex, the benzyl group of APE squeezes into and thereby widens the S4 specificity pocket of the peptidase, so that it is snugly accommodated in this enlarged pocket now formed by the residues 165 to 168, Phe185, Gln192 and the main-chain atoms of Val186 (Figures 3(b) and 4(c)).	./cache/cord-286537-7ri2p5b8.txt	./txt/cord-286537-7ri2p5b8.txt