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How USP 18 deals with ISG 15‐modified proteins: structural basis for the specificity of the protease
Author(s) -
Basters Anja,
Knobeloch KlausPeter,
Fritz Günter
Publication year - 2018
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14260
Subject(s) - protease , interferon , chemistry , ubiquitin , receptor , biochemistry , enzyme , microbiology and biotechnology , biology , gene , genetics
The ubiquitin‐specific protease 18 ( USP 18) has two major functions: (a) it is a highly specific protease that cleaves the ubiquitin‐like modifier ISG 15 (interferon‐stimulated gene 15) from proteins, and (b) independent from its enzymatic activity USP 18 interacts with the type I interferon receptor and shuts off downstream signaling. The structures of USP 18 and a USP 18– ISG 15 complex revealed the molecular basis of the unique specificity of the protease and might shed some light into its interaction with the interferon receptor.