Vascular endothelial growth factor receptor 2 kinase domain (VEGFR2 kinase domain)

The vascular endothelial growth factor receptor 2 kinase domain (VEGFR2 kinase domain) is the intracellular, enzymatically active portion of the full-length VEGFR2, a receptor tyrosine kinase. VEGFR2, encoded by the KDR gene, is a transmembrane glycoprotein predominantly expressed in vascular endothelial cells, where it mediates the effects of vascular endothelial growth factors (VEGF-A, VEGF-C, VEGF-D) to promote angiogenesis, vascular permeability, cell proliferation, and survival[1][2][3]. The kinase domain is composed of two lobes forming the active site, responsible for ATP binding and phosphotransfer reactions during intracellular signal transduction[1][7]. Ligand (VEGF) binding to the extracellular domains induces receptor dimerization and conformational changes, activating the kinase domain, leading to autophosphorylation and initiation of downstream signaling pathways[3][7]. Dysregulation of VEGFR2 signaling is implicated in pathologies such as cancer (tumor angiogenesis), inflammatory conditions, and certain ocular diseases[1][2]. Numerous small molecule inhibitors specifically target the VEGFR2 kinase domain to block these pathological signaling events. Structural and functional studies have demonstrated the importance of the kinase domain for both normal physiological angiogenesis and abnormal vessel growth in disease[2][7][4][6][8].

Other names

Kinase insert domain-containing receptor (KDR)Fetal liver kinase 1 (Flk-1; mouse ortholog)

Inhibition of receptor tyrosine kinase activity, Inhibition of angiogenic signaling, Blockade of ATP binding