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Xiaolan Yao, Samuel Bouyain  Structure 

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1 Splicing and Proteolytic Processing in VEGF Signaling: Now It Is the Coreceptor’s Turn 
Xiaolan Yao, Samuel Bouyain  Structure  Volume 23, Issue 4, Pages (April 2015) DOI: /j.str Copyright © 2015 Elsevier Ltd Terms and Conditions

2 Figure 1 Physiological Roles of VEGF-C and Its Sequestration by a Proteolyzed Isoform of Nrp2 (A) VEGF-C binds to VEGFR3 and Nrp2 to mediate angiogenesis and lymphangiogenesis. The cystine-knot region of VEGF-C (yellow) associates with VEGFR-3 while its C-terminal arginine residue mediates specific binding to Nrp2. (B) s9Nrp2B simultaneously engages the C-terminal arginine residues in the VEGF-C homodimer to sequester the growth factor and block Nrp2-based VEGF-C signaling. The formation of s9Nrp2B⋅VEGF-C complexes has no effect on the binding of VEGF-C to VEGFR3. Structure  , DOI: ( /j.str ) Copyright © 2015 Elsevier Ltd Terms and Conditions

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