Complementary and coordinated roles of the VEGFs and angiopoietins during normal and pathologic vascular formation

NW Gale, G Thurston, S Davis… - Cold Spring Harbor …, 2002 - symposium.cshlp.org
NW Gale, G Thurston, S Davis, SJ Wiegand, J Holash, JS Rudge, GD Yancopoulos
Cold Spring Harbor symposia on quantitative biology, 2002symposium.cshlp.org
Figure 1.(A) Schematic summary of interactions of VEGFs with their receptors, and of
angiopoietins with their Tie receptors.(B) On left, schematic view of angiopoietin monomer
indicating amino-terminal domain (N domain), coil-coil domain (C domain), and fibrinogen-
like domain (F domain). The F domain is the receptor-binding portion of this complex ligand,
whereas the C domain serves to dimerize two F domains, and the N domain acts to further
multimerize these dimers into tetramers, as shown on the right, or even higher-order …
Figure 1.(A) Schematic summary of interactions of VEGFs with their receptors, and of angiopoietins with their Tie receptors.(B) On left, schematic view of angiopoietin monomer indicating amino-terminal domain (N domain), coil-coil domain (C domain), and fibrinogen-like domain (F domain). The F domain is the receptor-binding portion of this complex ligand, whereas the C domain serves to dimerize two F domains, and the N domain acts to further multimerize these dimers into tetramers, as shown on the right, or even higher-order structures (not shown).
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