Dimerization of VEGF receptors and implications for signal transduction: a computational study.

ABSTRACT: Vascular endothelial growth factor (VEGF) is a potent cytokine involved in the induction of neovascularization. Secreted as a cysteine-linked dimer, it has two binding sites at opposite poles through which it may bind VEGF receptors (VEGFRs), receptor tyrosine kinases found on the surface of endothelial and other cells. The binding of a VEGF molecule to two VEGFR molecules induces transphosphorylation of the intracellular domains of the receptors, leading to signal transduction. The dominant mechanism of receptor dimerization is not clear: the receptors may be present in an inactive pre-dimerized form, VEGF binding first to one of the receptors, the second receptor then ideally located for dimerization; or VEGF may bind receptor monomers on the cell surface, which then diffuse and bind to

SUBMITTER: Mac Gabhann F 

PROVIDER: S-EPMC2711879 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature