2LMS

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

Summary for 2LMS

• Entry DOI: 10.2210/pdb2lms/pdb
• NMR Information: BMRB: 18135
• Descriptor: Interferon alpha-2, 2-acetamido-2-deoxy-alpha-D-galactopyranose (2 entities in total)
• Functional Keywords: cytokine, glycoprotein, o-glycosylation, signaling protein, type i interferons, immune system
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 19616.50

Authors

Ghasriani, H.,Belcourt, P.J.F.,Sauve, S.,Hodgson, D.J.,Gingras, G.,Brochu, D.,Gilbert, M.,Aubin, Y. (deposition date: 2011-12-12, release date: 2012-12-05, Last modification date: 2024-11-27)

Primary citation

Ghasriani, H.,Belcourt, P.J.,Sauve, S.,Hodgson, D.J.,Brochu, D.,Gilbert, M.,Aubin, Y.
A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon alpha2a around the glycosylation site.
J.Biol.Chem., 288:247-254, 2013

PubMed 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.

PubMed: 23184955
DOI: 10.1074/jbc.M112.413252

Experimental method

SOLUTION NMR