› 1pz7

X-ray diffraction
1.42Å resolution

Modulation of agrin function by alternative splicing and Ca2+ binding

Released:
DOI: 10.2210/pdb1pz7/pdb
PDB entry 1pz7 coloured by chain, front view.
PDB entry 1pz7 coloured by chain, side view.
PDB entry 1pz7 coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Modulation of agrin function by alternative splicing and Ca2+ binding.
Stetefeld J, Alexandrescu AT, Maciejewski MW, Jenny M, Rathgeb-Szabo K, Schulthess T, Landwehr R, Frank S, Ruegg MA, Kammerer RA
Structure 12 503-15 (2004)
PMID: 15016366

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-152071 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Agrin C-terminal 22 kDa fragment Chains: A, B
Molecule details ›
Chains: A, B
Length: 204 amino acids
Theoretical weight: 22.35 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P31696 (Residues: 1870-2081; Coverage: 10%)
Gene names: AGRIN, AGRN
Sequence domains: Laminin G domain
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: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: C2
Unit cell:
a: 101.329Å b: 57.54Å c: 74.621Å
α: 90° β: 127.1° γ: 90°
R-values:
R R work R free
0.221 0.22 0.24
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Proteoglycan form and function: A comprehensive nomenclature of proteoglycans.
Iozzo et al. (2015)
12 more

4 mentions without citation

Analysis of α-Dystroglycan/LG Domain Binding Modes: Investigating Protein Motifs That Regulate the Affinity of Isolated LG Domains.
Dempsey et al. (2019)
3 more