[HTML][HTML] Angiopoietin-1 and-2 coiled coil domains mediate distinct homo-oligomerization patterns, but fibrinogen-like domains mediate ligand activity
WN Procopio, PI Pelavin, WMF Lee… - Journal of Biological …, 1999 - ASBMB
Activity of endothelial Tie2 receptor tyrosine kinase is modulated by two naturally occurring,
secreted ligands, angiopoietin-1 and-2, which have opposing effects on its phosphorylation.
Receptor tyrosine kinase activation requires receptor dimerization/multimerization, which, for
many receptors, is mediated by homo-oligomeric ligands binding to and bridging receptor
molecules. We show here that angiopoietin-1 and-2 form distinct arrays of disulfide-linked
homo-oligomeric complexes. Their mobilities on nonreducing gels suggest that angiopoietin …
secreted ligands, angiopoietin-1 and-2, which have opposing effects on its phosphorylation.
Receptor tyrosine kinase activation requires receptor dimerization/multimerization, which, for
many receptors, is mediated by homo-oligomeric ligands binding to and bridging receptor
molecules. We show here that angiopoietin-1 and-2 form distinct arrays of disulfide-linked
homo-oligomeric complexes. Their mobilities on nonreducing gels suggest that angiopoietin …