Structure of a VEGF–VEGF receptor complex determined by electron microscopy
Copyright policy )Structure of a VEGF–VEGF receptor complex determined by electron microscopy
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.
- Paul Scherrer Institute Switzerland
- Harvard University United States
Vascular Endothelial Growth Factor A, Microscopy, Electron, Humans, Ligands, Dimerization, Vascular Endothelial Growth Factor Receptor-2, Protein Structure, Tertiary
Vascular Endothelial Growth Factor A, Microscopy, Electron, Humans, Ligands, Dimerization, Vascular Endothelial Growth Factor Receptor-2, Protein Structure, Tertiary
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