Author: Hao, Wei; Wojdyla, Justyna Aleksandra; Zhao, Rong; Han, Ruiyun; Das, Rajat; Zlatev, Ivan; Manoharan, Muthiah; Wang, Meitian; Cui, Sheng
Title: Crystal structure of Middle East respiratory syndrome coronavirus helicase Document date: 2017_6_26
ID: 0vxhgjss_21
Snippet: Structural comparison of nsp13 CH and hUpf1 CH in complex with Upf2 [34] revealed two hydrophobic pockets on the surface of nsp13 CH equivalent to Upf2 binding sites on Upf1 ( Fig 3D) . While pocket 1 highly resembles Upf2 α-helix binding site, the pocket 2 has a much shorter β6-β7 loop than the equivalent loop in Upf2 β-hairpin binding site of Upf1 (β5-β6 loop). Two hydrophobic pockets on CH domain may function as interaction interfaces fo.....
Document: Structural comparison of nsp13 CH and hUpf1 CH in complex with Upf2 [34] revealed two hydrophobic pockets on the surface of nsp13 CH equivalent to Upf2 binding sites on Upf1 ( Fig 3D) . While pocket 1 highly resembles Upf2 α-helix binding site, the pocket 2 has a much shorter β6-β7 loop than the equivalent loop in Upf2 β-hairpin binding site of Upf1 (β5-β6 loop). Two hydrophobic pockets on CH domain may function as interaction interfaces for other CoV replicase or cellular protein.
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