作者: Claudia Ruch , Georgios Skiniotis , Michel O Steinmetz , Thomas Walz , Kurt Ballmer-Hofer
DOI: 10.1038/NSMB1202
关键词:
摘要: 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 VEGF to membrane-distal immunoglobulin-like domains causes receptor dimerization and promotes further interaction between monomers through membrane-proximal 7. By this mechanism, VEGFR-2 can be communicated across membrane, activating intracellular kinase domains.