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. 2021 Jan-Jun:296:100212.
doi: 10.1016/j.jbc.2020.100212. Epub 2021 Jan 14.

How to extend your (polylactosamine) antennae

Matthew S Kimber  1
Affiliations

How to extend your (polylactosamine) antennae

Matthew S Kimber. J Biol Chem. 2021 Jan-Jun.

Abstract

The elongated antennae decorating eukaryotic glycans are built from polylactosamine repeats. Polylactosamine forms a lectin recognition site and also acts as a platform for presenting diverse additional modifications (e.g., terminal cell-surface antigens); it therefore plays important roles in cell adherence, development, and immunity. Two new papers present a detailed structural and mechanistic investigation of β1-3-N-acetylgucosaminyltransferase 2, a key enzyme in antennae synthesis. The resulting insights will also help decipher other members of GT31, the single largest human glycosyltransferase family.

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Conflict of interest statement

Conflict of interest The author declares that he has no conflicts of interest with the contents of this article.

Figures

Figure 1
Figure 1
The role and structure of B3GNT2.A, B3GNT and B4GAL collaborate to build polylactosamine antennae on N-glycans (shown) as well as O-glycans and glycolipids; these are then subjected to further modifications. B, a surface view of the UDP plus product complex structure of B3GNT2 (RCSB i.d.: 7JHN). The lower left panel shows a conceptual model of how this protein would be anchored to the Golgi membrane, while the right panel shows details of one protomer. C, key substrate and product complexes characterized in these works.
See this image and copyright information in PMC

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