› 1qu0

X-ray diffraction
2.35Å resolution

CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN

Released:
DOI: 10.2210/pdb1qu0/pdb
PDB entry 1qu0 coloured by chain, front view.
PDB entry 1qu0 coloured by chain, side view.
PDB entry 1qu0 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin.
Hohenester E, Tisi D, Talts JF, Timpl R
Mol Cell 4 783-92 (1999)
PMID: 10619025

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178803 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Laminin subunit alpha-2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 191 amino acids
Theoretical weight: 20.42 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: Q60675 (Residues: 2932-3118; Coverage: 6%)
Gene name: Lama2
Sequence domains: Laminin G domain
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand CA 4 x CA
Ligand SO4 7 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX7.2
Spacegroup: P21
Unit cell:
a: 42.22Å b: 112.89Å c: 117.4Å
α: 90° β: 92° γ: 90°
R-values:
R R work R free
0.229 0.229 0.255
Expression system: Not provided

Quick links

Citations

36 review citations

Form and function: the laminin family of heterotrimers.
Colognato et al. (2000)
35 more

8 mentions without citation

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