The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences
GalNAc transferases’ (GalNAc-Ts) catalytic domains are connected to a lectin domain through a flexible linker. Here the authors present a structural analysis of GalNAc-T4 that implicates the linker region as modulator of the orientations of the lectin domain, which in turn imparts substrate specific...
Guardado en:
Autores principales: | Matilde de las Rivas, Erandi Lira-Navarrete, Earnest James Paul Daniel, Ismael Compañón, Helena Coelho, Ana Diniz, Jesús Jiménez-Barbero, Jesús M. Peregrina, Henrik Clausen, Francisco Corzana, Filipa Marcelo, Gonzalo Jiménez-Osés, Thomas A. Gerken, Ramon Hurtado-Guerrero |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2017
|
Materias: | |
Acceso en línea: | https://doaj.org/article/96c013e274ef4775a780ce73240387ed |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Polypeptide-GalNAc-Transferase-13 Shows Prognostic Impact in Breast Cancer
por: Eugenia Fernandez, et al.
Publicado: (2021) -
Chemoenzymatic modular assembly of O-GalNAc glycans for functional glycomics
por: Shuaishuai Wang, et al.
Publicado: (2021) -
Roles of GalNAc-disialyl Lactotetraosyl Antigens in Renal Cancer Cells
por: Akiko Tsuchida, et al.
Publicado: (2018) -
Selection of GalNAc-conjugated siRNAs with limited off-target-driven rat hepatotoxicity
por: Maja M. Janas, et al.
Publicado: (2018) -
A GalNAc/Gal-specific lectin from the sea mussel Crenomytilus grayanus modulates immune response in macrophages and in mice
por: Oleg V. Chernikov, et al.
Publicado: (2017)