Author: Linlin Zhang; Daizong Lin; Yuri Kusov; Yong Nian; Qingjun Ma; Jiang Wang; Albrecht von Brunn; Pieter Leyssen; Kristina Lanko; Johan Neyts; Adriaan de Wilde; Eric J. Snijder; Hong Liu; Rolf Hilgenfeld
Title: Alpha-ketoamides as broad-spectrum inhibitors of coronavirus and enterovirus replication Document date: 2020_2_10
ID: 7n8p9okf_18
Snippet: In agreement with these observations, a good fit is observed between the P2 benzyl group of 11a and the S2 subsite of the SARS-CoV M pro as well as that of the CVB3 3C pro (Fig. 3a,c) . In contrast, the crystal structure of the complex between 11a and HCoV-NL63 M pro , against which the compound is inactive, demonstrates that the P2-benzyl group cannot fully enter the S2 pocket of the enzyme because of the restricted size of this site (Fig. 3b) ......
Document: In agreement with these observations, a good fit is observed between the P2 benzyl group of 11a and the S2 subsite of the SARS-CoV M pro as well as that of the CVB3 3C pro (Fig. 3a,c) . In contrast, the crystal structure of the complex between 11a and HCoV-NL63 M pro , against which the compound is inactive, demonstrates that the P2-benzyl group cannot fully enter the S2 pocket of the enzyme because of the restricted size of this site (Fig. 3b) .
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