› 5n30

X-ray diffraction
1.8Å resolution

Crystal structure of the V72I mutant of the mouse alpha-Dystroglycan N-terminal region

Released:
DOI: 10.2210/pdb5n30/pdb
PDB entry 5n30 coloured by chain, front view.
PDB entry 5n30 coloured by chain, side view.
PDB entry 5n30 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The effect of the pathological V72I, D109N and T190M missense mutations on the molecular structure of α-dystroglycan.
Covaceuszach S, Bozzi M, Bigotti MG, Sciandra F, Konarev PV, Brancaccio A, Cassetta A
OpenAccess logo PLoS One 12 e0186110 (2017)
PMID: 29036200

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178918 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-dystroglycan Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 28.31 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q62165 (Residues: 50-312; Coverage: 30%)
Gene name: Dag1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand EDO 3 x EDO
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: R3
Unit cell:
a: 71.81Å b: 71.81Å c: 143.99Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.156 0.154 0.182
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

A molecular overview of the primary dystroglycanopathies.
Brancaccio A. (2019)
3 other articles

1 mention without citation

The effect of the pathological V72I, D109N and T190M missense mutations on the molecular structure of α-dystroglycan.
Covaceuszach et al. (2017)