Structure of a VEGF-VEGF receptor complex determined by electron microscopy.
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 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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关键词：
Humans Vascular Endothelial Growth Factor Receptor-2 Vascular Endothelial Growth Factor A Ligands Microscopy, Electron Protein Structure, Tertiary Dimerization
DOI：
10.1038/nsmb1202
被引量：
年份：
2007
Springer
Nature
Semantic Scholar
Ingenta
dx.doi.org
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