Cargando…
Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation
Hsp104 is a ring-forming, ATP-driven molecular machine that recovers functional protein from both stress-denatured and amyloid-forming aggregates. Although Hsp104 shares a common architecture with Clp/Hsp100 protein unfoldases, different and seemingly conflicting 3D structures have been reported. Ex...
Autores principales: | Lee, Sukyeong, Roh, Soung Hun, Lee, Jungsoon, Sung, Nuri, Liu, Jun, Tsai, Francis T.F. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6347426/ https://www.ncbi.nlm.nih.gov/pubmed/30605683 http://dx.doi.org/10.1016/j.celrep.2018.12.037 |
Ejemplares similares
-
Structural determinants for protein unfolding and translocation by the Hsp104 protein disaggregase
por: Lee, Jungsoon, et al.
Publicado: (2017) -
Suramin Inhibits Hsp104 ATPase and Disaggregase Activity
por: Torrente, Mariana P., et al.
Publicado: (2014) -
Structural basis for the disaggregase activity and regulation of Hsp104
por: Heuck, Alexander, et al.
Publicado: (2016) -
Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation
por: Lee, Jungsoon, et al.
Publicado: (2017) -
The Schizosaccharomyces pombe Hsp104 Disaggregase Is Unable to Propagate the [PSI
(+)] Prion
por: Sénéchal, Patrick, et al.
Publicado: (2009)