› 2rcz

X-ray diffraction
1.7Å resolution

Structure of the second PDZ domain of ZO-1

Released:
DOI: 10.2210/pdb2rcz/pdb
PDB entry 2rcz coloured by chain, front view.
PDB entry 2rcz coloured by chain, side view.
PDB entry 2rcz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Domain swapping within PDZ2 is responsible for dimerization of ZO proteins.
Fanning AS, Lye MF, Anderson JM, Lavie A
J Biol Chem 282 37710-6 (2007)
PMID: 17928286

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170449 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tight junction protein ZO-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 81 amino acids
Theoretical weight: 9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07157 (Residues: 186-264; Coverage: 5%)
Gene names: TJP1, ZO1
Sequence domains: PDZ domain
Structure domains: Pdz3 Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 47.75Å b: 33.61Å c: 91.04Å
α: 90° β: 103.64° γ: 90°
R-values:
R R work R free
0.209 0.204 0.258
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Architecture of tight junctions and principles of molecular composition.
Van Itallie et al. (2014)
9 more

8 mentions without citation

Plasticity of PDZ domains in ligand recognition and signaling.
Ivarsson Y. (2012)
7 more