› 4deq

X-ray diffraction
2.65Å resolution

Structure of the Neuropilin-1/VEGF-A complex

Released:
DOI: 10.2210/pdb4deq/pdb
PDB entry 4deq coloured by chain, front view.
PDB entry 4deq coloured by chain, side view.
PDB entry 4deq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for selective vascular endothelial growth factor-A (VEGF-A) binding to neuropilin-1.
Parker MW, Xu P, Li X, Vander Kooi CW
J Biol Chem 287 11082-9 (2012)
PMID: 22318724

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127134 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuropilin-1; VEGFA Chains: A, B
Molecule details ›
Chains: A, B
Length: 218 amino acids
Theoretical weight: 24.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O14786 (Residues: 274-429; Coverage: 17%)
  • Canonical: P15692 (Residues: 346-395; Coverage: 13%)
Gene names: NRP, NRP1, VEGF, VEGF165R, VEGFA
Sequence domains: F5/8 type C domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P43
Unit cell:
a: 114.978Å b: 114.978Å c: 50.946Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.209 0.267
Expression system: Escherichia coli

Quick links

Citations

33 review citations

VEGF targets the tumour cell.
Goel et al. (2013)
32 more

32 mentions without citation

Molecular Pharmacology of VEGF-A Isoforms: Binding and Signalling at VEGFR2.
Peach et al. (2018)
31 more