2lms | pdb_00002lms

A single GalNAc residue on Threonine-106 modifies the dynamics and the structure of Interferon alpha-2a around the glycosylation site

spinqualitylabelsall models 2lms Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lms is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Ligands: A2G Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Enzymatic addition of GalNAc to isotopically labeled IFNalpha2a produced in Escherichia coli yielded the O-linked glycoprotein GalNAcalpha-[(13)C,(15)N]IFNalpha2a. The three-dimensional structure of GalNAcalpha-IFNalpha2a 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(beta1,3)GalNAcalpha-[(13)C,(15)N]IFNalpha2a. 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. A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon alpha2a around the glycosylation site.,Ghasriani H, Belcourt PJ, Sauve S, Hodgson DJ, Brochu D, Gilbert M, Aubin Y J Biol Chem. 2013 Jan 4;288(1):247-54. doi: 10.1074/jbc.M112.413252. Epub 2012, Nov 26. PMID:23184955 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Interferon 3D structures

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