Transmembrane domain-mediated orientation of receptor monomers in active VEGFR-2 dimers.

@article{Dosch2010TransmembraneDO,
  title={Transmembrane domain-mediated orientation of receptor monomers in active VEGFR-2 dimers.},
  author={Debora Dell'Era Dosch and Kurt Ballmer-Hofer},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2010},
  volume={24 1},
  pages={32-8}
}
Vascular endothelial growth factors (VEGFs) activate cellular receptor tyrosine kinases (RTKs) such as VEGFR-1, -2, and -3. These receptors are activated upon ligand binding to the extracellular receptor domain (ECD), resulting in receptor dimerization and activation of the intracellular kinase domain. Here we investigated the molecular mechanism of activation of the human VEGFR-2 expressed in human HEK293, monkey COS-1, and porcine aortic endothelial cells. To study the role of dimerization in… CONTINUE READING