Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD
The ER chaperone BiP is critical for the unfolded protein response and tightly regulated through reversible AMPylation by FICD, but the structural basis is unknown. Here the authors use thiol-reactive nucleotide derivatives to stabilize the transient FICD:BiP complex and determine its crystal struct...
Guardado en:
Autores principales: | Joel Fauser, Burak Gulen, Vivian Pogenberg, Christian Pett, Danial Pourjafar-Dehkordi, Christoph Krisp, Dorothea Höpfner, Gesa König, Hartmut Schlüter, Matthias J. Feige, Martin Zacharias, Christian Hedberg, Aymelt Itzen |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/5b881075f8d343709870eb7b338a3da3 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1
por: Jiqing Du, et al.
Publicado: (2021) -
FICD activity and AMPylation remodelling modulate human neurogenesis
por: Pavel Kielkowski, et al.
Publicado: (2020) -
Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD
por: Luke A. Perera, et al.
Publicado: (2021) -
Alberto Mozó: BIP Computers
por: Mozó,Alberto
Publicado: (2009) -
TPR-STORYTELLING. A key to speak fluently in english
por: NIDIA ROCÍO BERNAL NUMPAQUE, et al.
Publicado: (2010)