How USP18 deals with ISG15-modified proteins: structural basis for the specificity of the protease

被引：20

作者：

Basters, Anja ^{[1
]}

Knobeloch, Klaus-Peter ^{[1
]}

Fritz, Guenter ^{[1
]}

机构：

[1] Univ Freiburg, Inst Neuropathol, Fac Med, Freiburg, Germany

来源：

FEBS JOURNAL | 2018年 / 285卷 / 06期

关键词：

cysteine protease; interferon; ISG15; USP; DEUBIQUITINATING ENZYME; ISOPEPTIDASE ACTIVITY; CRYSTAL-STRUCTURE; CROSS-REACTIVITY; VIRAL RESISTANCE; ISG15; UBIQUITIN; INTERFERONOPATHY; DEFICIENCY; MECHANISMS;

D O I：

10.1111/febs.14260

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The ubiquitin-specific protease 18 (USP18) has two major functions: (a) it is a highly specific protease that cleaves the ubiquitin-like modifier ISG15 (interferon-stimulated gene 15) from proteins, and (b) independent from its enzymatic activity USP18 interacts with the type I interferon receptor and shuts off downstream signaling. The structures of USP18 and a USP18-ISG15 complex revealed the molecular basis of the unique specificity of the protease and might shed some light into its interaction with the interferon receptor.

引用

页码：1024 / 1029

页数：6

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