› 1vgh

Solution NMR

HEPARIN-BINDING DOMAIN FROM VASCULAR ENDOTHELIAL GROWTH FACTOR, NMR, 20 STRUCTURES

Released:
DOI: 10.2210/pdb1vgh/pdb
PDB entry 1vgh coloured by chain, ensemble of 20 models, front view.
PDB entry 1vgh coloured by chain, ensemble of 20 models, side view.
PDB entry 1vgh coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the heparin-binding domain of vascular endothelial growth factor.
Fairbrother WJ, Champe MA, Christinger HW, Keyt BA, Starovasnik MA
Structure 6 637-48 (1998)
PMID: 9634701

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147426 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vascular endothelial growth factor A, long form Chain: A
Molecule details ›
Chain: A
Length: 55 amino acids
Theoretical weight: 6.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15692 (Residues: 346-395; Coverage: 13%)
Gene names: VEGF, VEGFA
Structure domains: Vascular endothelial growth factor, heparin-binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DISTANCE GEOMETRY/ SIMULATED ANNEALING/RESTRAINED MOLECULAR DYNAMICS
Expression system: Escherichia coli

Quick links

Citations

23 review citations

Pegaptanib, a targeted anti-VEGF aptamer for ocular vascular disease.
Ng et al. (2006)
22 more

6 mentions without citation

A Structural Overview of Vascular Endothelial Growth Factors Pharmacological Ligands: From Macromolecules to Designed Peptidomimetics.
Ye et al. (2021)
5 more