article
How USP 18 deals with ISG 15‐modified proteins: structural basis for the specificity of the protease
Anja Bastersa b✉, Klaus‐Peter Knobelocha b, Günter Fritza b
- aFaculty of Medicine Institute of Neuropathology University of Freiburg Freiburg Germany
- bFaculty of Medicine, Institute of Neuropathology, University of Freiburg, Freiburg, Germany
- ✉Corresponding author
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Abstract
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.