2koh

Solution NMR

NMR structure of mouse Par3-PDZ3 in complex with VE-Cadherin C-terminus

Released:
Source organism: Mus musculus
Primary publication:
Distal interactions within the par3-VE-cadherin complex.
Biochemistry 49 951-7 (2010)
PMID: 20047332

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-157291 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Partitioning defective 3 homolog Chain: A
Molecule details ›
Chain: A
Length: 111 amino acids
Theoretical weight: 11.91 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99NH2 (Residues: 581-689; Coverage: 8%)
Gene names: Par3, Pard3
Sequence domains: PDZ domain
Structure domains: Pdz3 Domain
Cadherin-5 Chain: B
Molecule details ›
Chain: B
Length: 16 amino acids
Theoretical weight: 1.82 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P55284 (Residues: 769-784; Coverage: 2%)
Gene name: Cdh5

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: AUTOMATED METHODS WERE USED FOR BACKBONE CHEMICAL SHIFT ASSIGNMENT AND ITERATIVE NOE REFINEMENT. FINAL STRUCTURES WERE OBTAINED BY MOLECULAR DYNAMICS IN EXPLICIT SOLVENT
Expression system: Escherichia coli