2lms

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.