Related Experiment Video
Updated: Feb 23, 2026

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
Published on: January 26, 2024
How USP18 deals with ISG15-modified proteins: structural basis for the specificity of the protease
Anja Basters1, Klaus-Peter Knobeloch1, Günter Fritz1
1Faculty of Medicine, Institute of Neuropathology, University of Freiburg, Freiburg, Germany.
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.
More Related Videos
Related Concept Videos
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....
Regulation of the Unfolded Protein Response
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
Regulation of Nuclear Protein Sorting
Ligand Binding and Linkage
Directing Proteins to the Rough Endoplasmic Reticulum

