› 2m59

Solution NMR

Spatial structure of dimeric VEGFR2 membrane domain in DPC micelles

Released:
DOI: 10.2210/pdb2m59/pdb
PDB entry 2m59 coloured by chain, ensemble of 10 models, front view.
PDB entry 2m59 coloured by chain, ensemble of 10 models, side view.
PDB entry 2m59 coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional characterization of alternative transmembrane domain conformations in VEGF receptor 2 activation.
Manni S, Mineev KS, Usmanova D, Lyukmanova EN, Shulepko MA, Kirpichnikov MP, Winter J, Matkovic M, Deupi X, Arseniev AS, Ballmer-Hofer K
Structure 22 1077-1089 (2014)
PMID: 24980797

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153088 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vascular endothelial growth factor receptor 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 37 amino acids
Theoretical weight: 4.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35968 (Residues: 759-795; Coverage: 3%)
Gene names: FLK1, KDR, VEGFR2
Sequence domains: VEGFR-2 Transmembrane domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 47%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

4 mentions without citation

Structural Basis for Vascular Endothelial Growth Factor Receptor Activation and Implications for Disease Therapy.
Shaik et al. (2020)
3 more