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. Author manuscript; available in PMC: 2016 Apr 7.
Published in final edited form as: Structure. 2015 Mar 5;23(4):677–687. doi: 10.1016/j.str.2015.01.018

Figure 2. Mechanism of VEGF-C binding to Nrp2.

Figure 2

(A) Zoom of the intermolecular interface between Nrp2 (blue) and VEGF-C (green) with the 2Fo-Fc electron density map for VEGF-C contoured at 1.0σ. Interfacing water is shown as grey spheres. (B) Ligplot+ generated representation of the interaction between VEGF-C (green) and Nrp2 (blue). Bond distances (Å) are labeled in black and water is shown as grey spheres. (C) Nrp2 binding was compared between VEGF-C and VEGF-C R223E. Binding was measured in triplicate and is reported as mean ± SD (*p<0.05). (D) Superimposition of the VEGF-A HBD/Nrp1 complex (PDB=4DEQ) and the tuftsin/Nrp1 complex (PDB=2ORZ) onto the structure of the VEGF-C/Nrp2 complex demonstrates the shared and unique modes of engagement within this ligand/receptor family.