Journal article
Structure of a VEGF-VEGF receptor complex determined by electron microscopy.
- Ruch C Paul Scherrer Institut, Biomolecular Research, Molecular Cell Biology, CH-5232 Villigen-PSI, Switzerland.
- Skiniotis G
- Steinmetz MO
- Walz T
- Ballmer-Hofer K
- 2007-02-13
Published in:
- Nature structural & molecular biology. - 2007
Dimerization
Humans
Ligands
Microscopy, Electron
Protein Structure, Tertiary
Vascular Endothelial Growth Factor A
Vascular Endothelial Growth Factor Receptor-2
English
Receptor tyrosine kinases are activated upon ligand-induced dimerization. Here we show that the monomeric extracellular domain of vascular endothelial growth factor (VEGF) receptor-2 (VEGFR-2) has a flexible structure. Binding of VEGF to membrane-distal immunoglobulin-like domains causes receptor dimerization and promotes further interaction between receptor monomers through the membrane-proximal immunoglobulin-like domain 7. By this mechanism, ligand-induced dimerization of VEGFR-2 can be communicated across the membrane, activating the intracellular tyrosine kinase domains.
- Language
-
- English
- Open access status
- closed
- Identifiers
-
- DOI 10.1038/nsmb1202
- PMID 17293873
- Persistent URL
- https://sonar.ch/global/documents/13450
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