期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 14, 期 3, 页码 249-250出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1202
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资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P01GM062580] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM62580] Funding Source: Medline
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 immunoglobulinlike 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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