NDLI: A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon 2a around the glycosylation site.

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A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon 2a around the glycosylation site.

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A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon 2a around the glycosylation site.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Belcourt, Pascal J. F. Hodgson, Derek J. Sauvé, Simon Brochu, Denis Gilbert, Michel Aubin, Yves Ghasriani, Houman
Description	Author Affiliation: Ghasriani H ( Centre for Vaccine Evaluation, Biologics and Genetic Therapies Directorate, Health Canada, Ottawa, Ontario K1A 0K9, Canada.)
Abstract	Enzymatic addition of GalNAc to isotopically labeled IFN 2a produced in Escherichia coli yielded the O-linked glycoprotein GalNAc -[(13)C,(15)N]IFN 2a. The three-dimensional structure of GalNAc -IFN 2a 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(ß1,3)GalNAc -[(13)C,(15)N]IFN 2a. 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.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	1
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-01-04
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Acetylgalactosamine Chemistry Interferon-alpha Metabolism Polysaccharides Threonine Genetics Computational Biology Disulfides Escherichia Coli Glycoproteins Glycosylation Interferons Magnetic Resonance Spectroscopy Models, Molecular Molecular Conformation Peptides Protein Conformation Recombinant Proteins Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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