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Solution NMR

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

Released:
DOI: 10.2210/pdb2lms/pdb
PDB entry 2lms coloured by chain, ensemble of 20 models, front view.
PDB entry 2lms coloured by chain, ensemble of 20 models, side view.
PDB entry 2lms coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon α2a around the glycosylation site.
Ghasriani H, Belcourt PJ, Sauvé S, Hodgson DJ, Brochu D, Gilbert M, Aubin Y
J Biol Chem 288 247-54 (2013)
PMID: 23184955

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134391 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Interferon alpha-2 Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 19.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P01563 (Residues: 24-188; Coverage: 100%)
Gene names: IFNA2, IFNA2A, IFNA2B, IFNA2C
Sequence domains: Interferon alpha/beta domain
Structure domains: Growth Hormone; Chain: A;

Ligands and Environments

1 bound ligand:
Ligand A2G 1 x A2G
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 90%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Mammalian protein glycosylation--structure versus function.
Defaus et al. (2014)
1 more

3 mentions without citation

O-glycosylation and its role in therapeutic proteins.
Thompson et al. (2022)
2 more