Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle

Chaperonins are ubiquitous protein assemblies present in bacteria, eukaryota, and archaea, facilitating the folding of proteins, preventing protein aggregation, and thus participating in maintaining protein homeostasis in the cell. During their functional cycle, they bind unfolded client proteins in...

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Detalles Bibliográficos
Autores principales: Mas, Guillaume, Guan, Jia-Ying, Crublet, Elodie, Debled, Elisa Colas, Moriscot, Christine, Gans, Pierre, Schoehn, Guy, Macek, Pavel, Schanda, Paul, Boisbouvier, Jerome
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2018
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6154984/
https://www.ncbi.nlm.nih.gov/pubmed/30255156
http://dx.doi.org/10.1126/sciadv.aau4196

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6154984/
https://www.ncbi.nlm.nih.gov/pubmed/30255156
http://dx.doi.org/10.1126/sciadv.aau4196

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