Localization of heparin- and neuropilin-1-recognition sites of viral VEGFs.
VEGF-A165 plays a central role in neovascularization. The biological activities of VEGF-A165 are largely mediated through KDR. VEGF-A165 also binds to cellular coreceptors, neuropilin-1 (NP-1), and heparin, via its C-terminal domain, resulting in functional modulation. Parapoxvirus-encoded VEGFs (PV-VEGFs), which recognize KDR, possess basic amino acid clusters in their C-terminal regions. Some PV-VEGFs may interact with NP-1; however, the NP-1- and heparin-binding properties have not been fully characterized. Here, we demonstrate that the heparin- and NP-1-binding region of PV-VEGFs is located in its C-terminal tail. Furthermore, the two arginine residues adjacent to the C-terminus greatly contribute to both interactions.
Tokunaga
Yuko
Y
Department of Biochemistry, Meiji Pharmaceutical University, 2-522-1, Noshio, Kiyose, Tokyo 204-8588, Japan.
Yamazaki
Yasuo
Y
Morita
Takashi
T
D001665:Binding Sites; D006493:Heparin / Q000378:metabolism*; D039942:Neuropilin-1 / Q000378:metabolism*; D018157:Parapoxvirus / Q000737:chemistry / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D042442:Vascular Endothelial Growth Factors / Q000737:chemistry / Q000378:metabolism*
D010446:Peptide Fragments; D042442:Vascular Endothelial Growth Factors; D039942:Neuropilin-1; D006493:Heparin