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. 2017 Jul 17;7:5525. doi: 10.1038/s41598-017-05876-y

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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(A) Sequence alignment of recombinant VEGF-A and Vammin proteins. Basic amino acids are in blue and acidic in red background. The last four amino acids expected to be important for NRP-1 binding are in black boxes. (B) VEGFR-1 competition binding assay (C) VEGFR-2 competition binding assay (D) NRP-1 binding into VEGF coated plates the presence of heparin (solid lines) and without heparin (dotted lines) (E) Heparin binding in VEGF coated plates (F). BaF3-VEGFR-2 proliferation assay. In B to F the values are expressed as mean ± SD. (G) Binding of the two C-terminal amino acids into the NRP-1 binding pocket. RR and PR sequences are drawn based on VEGF-A₁₆₅/NRP-1 and Tuftsin/NRP-1 complex structures. (PDB IDs 4DEQ and 2ORZ). RK sequence is modeled based on VEGF-A₁₆₅/NRP-1 complex structure. Ligand amino acids are shown as sticks and NRP-1 as surface rendering colored by interpolated charge. (H) A model of location of the Vammin_PRRK C-terminus. Vammin crystal structure (PDB ID 1 WQ8) was superimposed onto VEGF-C/VEGFR-2 complex crystal structure (PDB ID 2X1W). The two VEGFR-2 monomers are seen with the brown colors and the two antiparallel dimer forming Vammin chains with green and blue. The C-terminal Arg97 and Lys98 of Vammin projecting outward from the complex are shown as sticks.