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Updated: Jul 17, 2026

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy
Published on: September 11, 2015
Structure of a VEGF-VEGF receptor complex determined by electron microscopy
Claudia Ruch1, Georgios Skiniotis, Michel O Steinmetz
1Paul Scherrer Institut, Biomolecular Research, Molecular Cell Biology, CH-5232 Villigen-PSI, Switzerland.
Abstract:
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.
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