› 1dyk

X-ray diffraction
2Å resolution

Laminin alpha 2 chain LG4-5 domain pair

Released:
DOI: 10.2210/pdb1dyk/pdb
PDB entry 1dyk coloured by chain, front view.
PDB entry 1dyk coloured by chain, side view.
PDB entry 1dyk coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin.
Tisi D, Talts JF, Timpl R, Hohenester E
EMBO J 19 1432-40 (2000)
PMID: 10747011

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178803 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Laminin subunit alpha-2 Chain: A
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 42.74 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: Q60675 (Residues: 2730-3118; Coverage: 13%)
Gene name: Lama2
Sequence domains:
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: C2221
Unit cell:
a: 70.6Å b: 111.5Å c: 124.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.233 0.261
Expression system: Homo sapiens

Quick links

Citations

28 review citations

Expression and function of laminins in the embryonic and mature vasculature.
Hallmann et al. (2005)
27 more

9 mentions without citation

Laminin 332 processing impacts cellular behavior.
Rousselle et al. (2013)
8 more