z-logo
Premium
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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here