VEGFR-2–interacting residues are conserved between VEGF-C and VEGF-D. (A). A close-up of the VEGF-D Leu99 and Asp103 in the VEGF-D superposition with VEGF-C in the complex with VEGFR2-D23. VEGF-D (magenta), VEGF-C (orange), and VEGFR-2 (gray) are shown as a cartoon loop representation. VEGF-C Leu119 and Asp123 interactions with VEGFR-2 are shown along with the VEGF-D counterparts Leu99 and Asp103. VEGF-C and VEGFR-2 numbering are used. Hydrophobic and hydrophilic interactions are shown in gray and red dashed line, respectively. (B) A close-up of the L2 residues as in panel A. VEGF-C Glu169 and Asn167 and its VEGF-D counterparts Glu149 and Asn147 are shown in sticks. VEGF-C Glu169 interactions with VEGFR-2 Asn253 and Lys281 are shown. (C) VEGF-D hydrophobic residues in L1 and L3 and in the N-terminal helix are shown as yellow sticks. The 2 VEGF-D monomers in the homodimer are shown in light and dark gray in a cartoon loop representation. (D) A molecular surface model of the same as in panel C. Only the side chain surface is shown for the hydrophobic (yellow) residues.