Cargando…
Structure of protein O-mannose kinase reveals a unique active site architecture
The ‘pseudokinase’ SgK196 is a protein O-mannose kinase (POMK) that catalyzes an essential phosphorylation step during biosynthesis of the laminin-binding glycan on α-dystroglycan. However, the catalytic mechanism underlying this activity remains elusive. Here we present the crystal structure of Dan...
Autores principales: | Zhu, Qinyu, Venzke, David, Walimbe, Ameya S, Anderson, Mary E, Fu, Qiuyu, Kinch, Lisa N, Wang, Wei, Chen, Xing, Grishin, Nick V, Huang, Niu, Yu, Liping, Dixon, Jack E, Campbell, Kevin P, Xiao, Junyu |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5142810/ https://www.ncbi.nlm.nih.gov/pubmed/27879205 http://dx.doi.org/10.7554/eLife.22238 |
Ejemplares similares
-
Structure of Fam20A reveals a pseudokinase featuring a unique disulfide pattern and inverted ATP-binding
por: Cui, Jixin, et al.
Publicado: (2017) -
POMK regulates dystroglycan function via LARGE1-mediated elongation of matriglycan
por: Walimbe, Ameya S, et al.
Publicado: (2020) -
N-terminal domain on dystroglycan enables LARGE1 to extend matriglycan on α-dystroglycan and prevents muscular dystrophy
por: Okuma, Hidehiko, et al.
Publicado: (2023) -
A secretory kinase complex regulates extracellular protein phosphorylation
por: Cui, Jixin, et al.
Publicado: (2015) -
Relief of autoinhibition by conformational switch explains enzyme activation by a catalytically dead paralog
por: Volkov, Oleg A, et al.
Publicado: (2016)