› 4bsk

X-ray diffraction
4.2Å resolution

Crystal structure of VEGF-C in complex with VEGFR-3 domains D1-2

Released:
DOI: 10.2210/pdb4bsk/pdb
PDB entry 4bsk coloured by chain, front view.
PDB entry 4bsk coloured by chain, side view.
PDB entry 4bsk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and mechanistic insights into VEGF receptor 3 ligand binding and activation.
Leppänen VM, Tvorogov D, Kisko K, Prota AE, Jeltsch M, Anisimov A, Markovic-Mueller S, Stuttfeld E, Goldie KN, Ballmer-Hofer K, Alitalo K
Proc Natl Acad Sci U S A 110 12960-5 (2013)
PMID: 23878260

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153056 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Vascular endothelial growth factor receptor 3 Chain: A
Molecule details ›
Chain: A
Length: 214 amino acids
Theoretical weight: 23.86 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P35916 (Residues: 23-229; Coverage: 15%)
Gene names: FLT4, VEGFR3
Sequence domains: Vascular endothelial growth factor receptor 1-like, Ig-like domain
Vascular endothelial growth factor C Chain: C
Molecule details ›
Chain: C
Length: 121 amino acids
Theoretical weight: 13.59 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P49767 (Residues: 103-215; Coverage: 29%)
Gene name: VEGFC
Sequence domains: PDGF/VEGF domain

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand NAG 4 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I23
Unit cell:
a: 166.66Å b: 166.66Å c: 166.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.338 0.334 0.372
Expression system: Spodoptera frugiperda

Quick links

Citations

20 review citations

Vascular endothelial growth factor signaling in development and disease.
Karaman et al. (2018)
19 more

7 mentions without citation

The cellular response to vascular endothelial growth factors requires co-ordinated signal transduction, trafficking and proteolysis.
Smith et al. (2015)
6 more