| DOI | Resolve DOI: https://doi.org/10.1074/jbc.M112.413252 |
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| Author | Search for: Ghasriani, H.; Search for: Belcourt, P.J.F.; Search for: Sauvé, S.; Search for: Hodgson, D.J.; Search for: Brochu, D.1; Search for: Gilbert, M.1; Search for: Aubin, Y. |
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| Affiliation | - National Research Council of Canada. NRC Institute for Biological Sciences
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| Format | Text, Article |
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| Subject | enhancement measurements; heteronuclear; high resolution; isotopically labeled; O-linked glycoproteins; structure and dynamics; three-dimensional structure; time-scales; amino acids; dynamics; Escherichia coli; esterification; glucose; glycosylation; nuclear magnetic resonance spectroscopy; NMR spectroscopy; glycoproteins; alpha2a interferon; monosaccharide; n acetylgalactosamine; n acetylgalactosamine[13c,15n]alpha2a interferon; threonine; unclassified drug; addition reaction; biological activity; in vitro study; isotope labeling; molecular dynamics; nuclear magnetic resonance spectroscopy; protein analysis; protein glycosylation; protein metabolism; protein polymorphism; protein structure; protein synthesis; acetylgalactosamine; computational biology; disulfides; interferon-alpha; interferons; models, molecular; molecular conformation; peptides; polysaccharides; protein conformation; recombinant proteins |
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| Abstract | Enzymatic addition of GalNAc to isotopically labeled IFNα2a produced in Escherichia coli yielded the O-linked glycoprotein GalNAcα-[ 13C,15N]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[13C,15N]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. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc. |
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| Publication date | 2013 |
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| Publisher | American Society for Biochemistry and Molecular Biology |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 21269591 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | a8489825-4f72-4abc-8993-a85c2b2984fa |
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| Record created | 2013-12-13 |
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| Record modified | 2022-11-18 |
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