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Article

Structure of protein O-mannose kinase reveals a unique active site architecture.

eLife - 23 Nov 2016

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

Abstract excerpt

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 Danio rerio POMK in complex with Mg2+ ions, ADP, aluminum fluoride, and the GalNAc-β3-GlcNAc-β4-Man trisaccharide...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 27879205
DOI: 10.7554/eLife.22238
PMCID: PMC5142810

Genes

POMK

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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