id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-299994-1ksfo0pr	Kanitz, Manuel	Structural basis for catalysis and substrate specificity of a 3C-like cysteine protease from a mosquito mesonivirus	2019-05-02		.txt	text/plain	8934	450	59	In CavV and most other members of the genus Alphamesonivirus, the P2 position of putative 3CL pro substrates is predominantly occupied by Asn. The crystal structure of the 3CL pro /inhibitor complex shows that the Asn side chain fits perfectly into the S2 subpocket, with its carboxamide functionality acting as hydrogen bond donor and acceptor in interactions with the main chain carbonyl oxygen of Asp216 and the Oγ atom of Ser52, respectively. In the first crystal structure reported for a coronavirus 3CL pro , this Asp (Asp186 in the TGEV 3CL pro sequence) was found to form a hydrogen bond to a water molecule located in a position that, in chymotrypsin and related serine proteases, is occupied by the side chain of the third member of the catalytic triad (typically Asp) (Anand et al., 2002) .	./cache/cord-299994-1ksfo0pr.txt	./txt/cord-299994-1ksfo0pr.txt