› 1okq

X-ray diffraction
2.8Å resolution

LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR, CA1 SITE MUTANT

Released:
DOI: 10.2210/pdb1okq/pdb
PDB entry 1okq coloured by chain, front view.
PDB entry 1okq coloured by chain, side view.
PDB entry 1okq coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Distinct requirements for heparin and alpha-dystroglycan binding revealed by structure-based mutagenesis of the laminin alpha2 LG4-LG5 domain pair.
Wizemann H, Garbe JH, Friedrich MV, Timpl R, Sasaki T, Hohenester E
J Mol Biol 332 635-42 (2003)
PMID: 12963372

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: 42.66 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 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2221
Unit cell:
a: 70.11Å b: 110.734Å c: 123.835Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.27
Expression system: Homo sapiens

Quick links

Citations

19 review citations

Basement membranes: cell scaffoldings and signaling platforms.
Yurchenco PD. (2011)
18 more

4 mentions without citation

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