› 1qsv

Solution NMR

THE VEGF-BINDING DOMAIN OF FLT-1, 20 NMR STRUCTURES

Released:
DOI: 10.2210/pdb1qsv/pdb
PDB entry 1qsv coloured by chain, ensemble of 20 models, front view.
PDB entry 1qsv coloured by chain, ensemble of 20 models, side view.
PDB entry 1qsv coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the VEGF-binding domain of Flt-1: comparison of its free and bound states.
Starovasnik MA, Christinger HW, Wiesmann C, Champe MA, de Vos AM, Skelton NJ
J Mol Biol 293 531-44 (1999)
PMID: 10543948

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148220 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vascular endothelial growth factor receptor 1 Chain: A
Molecule details ›
Chain: A
Length: 101 amino acids
Theoretical weight: 11.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17948 (Residues: 129-229; Coverage: 8%)
Gene names: FLT, FLT1, FRT, VEGFR1
Sequence domains: Vascular endothelial growth factor receptor 1-like, Ig-like domain
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

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

Quick links

Citations

9 review citations

VEGF-A splicing: the key to anti-angiogenic therapeutics?
Harper et al. (2008)
8 more

2 mentions without citation

β-hairpin peptide that targets vascular endothelial growth factor (VEGF) receptors: design, NMR characterization, and biological activity.
Diana et al. (2011)
1 more