Activation dynamics of ubiquitin-specific protease 7.

ABSTRACT: Ubiquitin-specific protease 7 (USP7) is a deubiquitinating enzyme that plays a crucial role in cellular processes, including the maintenance of genome stability and regulation of antiviral and immune responses. Its dysfunction is linked to various cancers and neurodevelopmental disorders such as Hao-Fountain syndrome. Unlike other USP-family enzymes, the triad of catalytic residues in USP7 adopts an inactive conformation and undergoes rearrangement into the active state upon substrate binding. Despite its potential importance for regulating the enzyme's activity, the dynamics of USP7 have not been explored. In this study, we combine advanced CPMG NMR relaxation dispersion measurements with the analysis of enzyme kinetics to investigate the conformational dynamics of USP7 in solution and it

SUBMITTER: Valles GJ 

PROVIDER: S-EPMC12130818 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature