Structural insights into the species preference of the influenza B virus NS1 protein in ISG15 binding
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Dear Editor,Type Ⅰ interferons (IFNs) are secreted in the context of viral infection and mediate the expression of more than 300 IFN-stimulated genes (Schoggins and Rice,2011).One of the earliest and most highly induced ISGs is IFN-stimulated gene 15 (ISG15),a ubiquitin-like protein (Ubl) comprising two Ubl domains connected by a linker (Farrell et al.,1979;Haas et al.,1987;Narasimhan et al.,2005).Similar to ubiquitin,ISG15 can be covalently attached to lysine on numerous target proteins via its C-terminal LRLRGG sequence in a process called ISGylation,which is catalyzed by the E1-activating enzyme Ube1L,the E2 conjugating enzyme UbcH8 and E3 ligases such as human HerC5 and mouse HerC6 (Hermann and Bogunovic,2016).
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We thank the scientists at the SSRF beamline BL17U for assistance with diffraction data collection.We are grateful for the technical support provided by Dongli Wang.This work was supported by the National Natural Science Foundation of ChinaGrant .31470751 and U1405228 to Xinquan Wang;the Beijing Advanced Innovation Center for Structural Biology