› 2mk7

Solution NMR

Tetra-O-GalNAc glycosylated mucin sequence from alpha dystroglycan mucin domain

Released:
DOI: 10.2210/pdb2mk7/pdb
PDB entry 2mk7 coloured by chain, ensemble of 16 models, front view.
PDB entry 2mk7 coloured by chain, ensemble of 16 models, side view.
PDB entry 2mk7 coloured by chain, ensemble of 16 models, top view.
Source organism: Homo sapiens
Primary publication:
Contrasting the conformational effects of α-O-GalNAc and α-O-Man glycan protein modifications and their impact on the mucin-like region of alpha-dystroglycan.
Borgert A, Foley BL, Live D
Glycobiology 31 649-661 (2021)
PMID: 33295623

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171921 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-dystroglycan Chain: A
Molecule details ›
Chain: A
Length: 11 amino acids
Theoretical weight: 996 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q14118 (Residues: 418-427; Coverage: 1%)
Gene name: DAG1

Ligands and Environments

1 bound ligand:
Ligand A2G 4 x A2G
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 91%
Refinement method: simulated annealing
Expression system: Not provided

Quick links

Citations

3 citation in other articles

O-Glycan-Dependent Interaction between MUC1 Glycopeptide and MY.1E12 Antibody by NMR, Molecular Dynamics and Docking Simulations.
Kokubu et al. (2022)
2 more

3 mentions without citation

Plant Lectins Targeting O-Glycans at the Cell Surface as Tools for Cancer Diagnosis, Prognosis and Therapy.
Poiroux et al. (2017)
2 more