› 4qdq

X-ray diffraction
1.95Å resolution

Physical basis for Nrp2 ligand binding

Released:
DOI: 10.2210/pdb4qdq/pdb
PDB entry 4qdq coloured by chain, front view.
PDB entry 4qdq coloured by chain, side view.
PDB entry 4qdq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for VEGF-C binding to neuropilin-2 and sequestration by a soluble splice form.
Parker MW, Linkugel AD, Goel HL, Wu T, Mercurio AM, Vander Kooi CW
Structure 23 677-87 (2015)
PMID: 25752543

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-129982 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuropilin-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 329 amino acids
Theoretical weight: 37.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60462 (Residues: 276-595; Coverage: 35%)
Gene names: NRP2, VEGF165R2
Sequence domains: F5/8 type C domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

2 bound ligands:
Ligand GOL 4 x GOL
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 41.047Å b: 120.808Å c: 69.837Å
α: 90° β: 103.29° γ: 90°
R-values:
R R work R free
0.211 0.21 0.241
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Multifaceted Role of Neuropilins in the Immune System: Potential Targets for Immunotherapy.
Roy et al. (2017)
14 more

5 mentions without citation

Neuropilin Functions as an Essential Cell Surface Receptor.
Guo et al. (2015)
4 more