ArticleThe Journal of biological chemistry2013
A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon α2a around the glycosylation site.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- NMR Chemical Shift Prediction of Glycopeptides and Glycoproteins Aided by the Computer Program CASPER.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Cyanobacterial Production of Biopharmaceutical and Biotherapeutic Proteins.Frontiers in plant science · 2020Article
- Molecular cloning and transcriptional regulation of Indian peafowl (Pavo cristatus) IFN-α gene.Cell stress & chaperones · 2019Article
- Effects of localized interactions and surface properties on stability of protein-based therapeutics.The Journal of pharmacy and pharmacology · 2018Review
- Compatible topologies and parameters for NMR structure determination of carbohydrates by simulated annealing.PloS one · 2017Article
- Article
- Preparation of legionaminic acid analogs of sialo-glycoconjugates by means of mammalian sialyltransferases.Glycoconjugate journal · 2015Article
- Structural Insights into the Neutralization Properties of the Fully Human, Anti-interferon Monoclonal Antibody Sifalimumab.The Journal of biological chemistry · 2015Article
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Authors and funding
7 authors.
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Abstract
Enzymatic addition of GalNAc to isotopically labeled IFNα2a produced in Escherichia coli yielded the O-linked glycoprotein GalNAcα-[(13)C,(15)N]IFNα2a. The three-dimensional structure of GalNAcα-IFNα2a has been determined in solution by NMR spectroscopy at high resolution. Proton-nitrogen heteronuclear Overhauser enhancement measurements revealed that the addition of a single monosaccharide unit at Thr-106 significantly slowed motions of the glycosylation loop on the nanosecond time scale. Subsequent addition of a Gal unit produced Gal(β1,3)GalNAcα-[(13)C,(15)N]IFNα2a. This extension resulted in a further decrease in the dynamics of this loop. The methodology used here allowed the first such description of the structure and dynamics of an O-glycoprotein and opens the way to the study of this class of proteins.
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