Fig. 8
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- ZDB-FIG-240703-73
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- Choleva et al., 2024 - Targeting the interaction of pleiotrophin and VEGFA165 with protein tyrosine phosphatase receptor zeta 1 inhibits endothelial cell activation and angiogenesis
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Molecular Docking Calculations. (A) Residue sequences for PTPRZ1, VEGFA residues 219–313 (PDB: 3v2a) and 346-295 (PDB: 4deq) and PTN. The residues that are mainly involved in the binding interactions as predicted for the PTN/PTPRZ1 (black) and VEGFA/PTPRZ1 (red for residues 219–313 and blue for residues 346–395) complexes by the PRODIGY tool are shown in boxes. The numbering for the two VEGFA regions (3v2a and 4deq) corresponds to the canonical sequence of VEGFA (Uniprot ID: P15692). The numbering of PTN corresponds to the mature protein following the removal of the signaling peptide (Uniprot ID: P21246). The numbering of PTPRZ1 FNIII corresponds to the canonical sequence of PTPRZ1 (Uniprot ID: 23471/PDB ID:8fn8). (B) Interaction between PTN (yellow) and PTPRZ1 (green) as predicted by HADDOCK molecular docking. The magenta-colored residues represent the PTN residues that are primarily involved in the interaction between the two proteins. |
Reprinted from European Journal of Pharmacology, 977, Choleva, E., Menounou, L., Ntenekou, D., Kastana, P., Tzoupis, Η., Katraki-Pavlou, S., Drakopoulou, M., Spyropoulos, D., Andrikopoulou, A., Kanellopoulou, V., Enake, M.K., Beis, D., Papadimitriou, E., Targeting the interaction of pleiotrophin and VEGFA165 with protein tyrosine phosphatase receptor zeta 1 inhibits endothelial cell activation and angiogenesis, 176692, Copyright (2024) with permission from Elsevier. Full text @ Eur. J. Pharmacol.