Cargando…
Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain
USP4 is a member of the ubiquitin-specific protease (USP) family of deubiquitinating enzymes that has a role in spliceosome regulation. Here, we show that the crystal structure of the minimal catalytic domain of USP4 has the conserved USP-like fold with its typical ubiquitin-binding site. A ubiquiti...
Autores principales: | Luna-Vargas, Mark P A, Faesen, Alex C, van Dijk, Willem J, Rape, Michael, Fish, Alexander, Sixma, Titia K |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
European Molecular Biology Organization
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3077250/ https://www.ncbi.nlm.nih.gov/pubmed/21415856 http://dx.doi.org/10.1038/embor.2011.33 |
Ejemplares similares
-
The DUSP–Ubl domain of USP4 enhances its catalytic efficiency by promoting ubiquitin exchange
por: Clerici, Marcello, et al.
Publicado: (2014) -
Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation
por: Maspero, Elena, et al.
Publicado: (2011) -
Target Specificity of the E3 Ligase LUBAC for Ubiquitin and NEMO Relies on Different Minimal Requirements
por: Smit, Judith J., et al.
Publicado: (2013) -
Structure and Catalytic Regulatory Function of Ubiquitin
Specific Protease 11 N-Terminal and Ubiquitin-like Domains
por: Harper, Stephen, et al.
Publicado: (2014) -
The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension
por: Smit, Judith J, et al.
Publicado: (2012)