The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry
Link
http://www.nature.com/articles/s41467-017-02006-0.pdf
Reference37 articles.
1. Bennett, E. P. et al. Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family. Glycobiology 22, 736–756 (2012).
2. Gill, D. J., Clausen, H. & Bard, F. Location, location, location: new insights into O-GalNAc protein glycosylation. Trends Cell Biol. 21, 149–158 (2011).
3. Hurtado-Guerrero, R. Recent structural and mechanistic insights into protein O-GalNAc glycosylation. Biochem. Soc. Trans. 44, 61–67 (2016).
4. Lira-Navarrete, E. et al. Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation. Nat. Commun. 6, 6937 (2015).
5. Tabak, L. A. The role of mucin-type O-glycans in eukaryotic development. Semin. Cell Dev. Biol. 21, 616–621 (2010).
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