O-Glycosylated Thr106.
The OG1 of Thr106 is covalently attached to D-Gal-beta(1-3)GalNAc via the C1 of GalNAc (N-Acetyl-D-Galactosamine) in axial form (alpha anomer).

A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon α2a around the glycosylation site.

Nmr Based Docking Model Of The Complex Between The Human Type I Interferon Receptor And Human Interferon Alpha-2

Inter-Molecular Interactions In A 44 Kda Interferon-Receptor Complex Detected By Asymmetric Back-Protonation And 2d Noesy

Structure Of The 44 Kda Complex Of Interferon-Alpha2 With The Extracellular Part Of Ifnar2 Obtained By 2d-Double Difference Noe

A Single Galnac Residue On Threonine-106 Modifies The Dynamics And The Structure Of Interferon Alpha-2a Around The Glycosylatio

Structural Insights Into The Neutralization Properties Of A Human Anti-interferon Monoclonal Antibody

interferon, alpha 2 [synthetic construct]

interferon alpha-2 precursor [Homo sapiens]

unnamed protein product [synthetic construct]

leukocytic interferon alpha-2 [synthetic construct]

alpha 2 interferon, partial [Homo sapiens]

interferon alpha 2b- 44LQ [synthetic construct]

PREDICTED: interferon alpha-2 [Pan paniscus]

PREDICTED: interferon alpha-2 [Gorilla gorilla gorilla]

PREDICTED: interferon alpha-2 [Pan troglodytes]

RecName: Full=Interferon alpha-2; Short=IFN-alpha-2; AltName: Full=Interferon alpha-A; Short=LeIF A; Flags: Precursor

The N-terminal His-tag of the protein (10 Histidines) was cleaved and removed before glycosylation and prior to NMR experiments.

Interferon Alpha-2a, where Thr106 is glycosylated with a 2-unit saccharide moiety, a Gal-GalNac.

Interferon Alpha-2A, with GalNac at Thr106.

Buffer: 25mM deuturated sodium acetate (NaOAc, d3) at pH 3.5.