Cargando…
1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain
The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. Th...
Autores principales: | Singh, Chingakham R., Lovell, Scott, Mehzabeen, Nurjahan, Chowdhury, Wasimul Q., Geanes, Eric S., Battaile, Kevin P., Roelofs, Jeroen |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3976055/ https://www.ncbi.nlm.nih.gov/pubmed/24699731 http://dx.doi.org/10.1107/S2053230X14003884 |
Ejemplares similares
-
Reconfiguration of the proteasome during chaperone-mediated assembly
por: Park, Soyeon, et al.
Publicado: (2013) -
Monellin (MNEI) at 1.15 Å resolution
por: Hobbs, J. R., et al.
Publicado: (2007) -
The penultimate step of proteasomal ATPase assembly is mediated by a switch dependent on the chaperone Nas2
por: Sekaran, Suganya, et al.
Publicado: (2023) -
Misfolding of Proteins with a Polyglutamine Expansion Is Facilitated by
Proteasomal
Chaperones
por: Rousseau, Erwann, et al.
Publicado: (2009) -
Assembly chaperone Nas6 selectively destabilizes 26S proteasomes with defective regulatory particle-core particle interfaces
por: Warnock, Jennifer L., et al.
Publicado: (2023)