 |
Journal articles
Biophysical Studies of the Induced Dimerization of Human VEGF Receptor 1 Binding Domain by Divalent Metals Competing with VEGF-A
Abstract : Angiogenesis is tightly regulated through the binding of vascular endothelial growth factors (VEGFs) to their receptors (VEGFRs). In this context, we showed that human VEGFR1 domain 2 crystallizes in the presence of Zn 2+ , Co 2+ or Cu 2+ as a dimer that forms via metal-ion interactions and interlocked hydrophobic surfaces. SAXS, NMR and size exclusion chromatography analyses confirm the formation of this dimer in solution in the presence of Co 2+ , Cd 2+ or Cu 2+ . Since the metal-induced dimerization masks the VEGFs binding surface, we investigated the ability of metal ions to displace the VEGF-A binding to hVEGFR1: using a competition assay, we evidenced that the metals displaced the VEGF-A binding to hVEGFR1 extracellular domain binding at micromolar level.
Cited literature [74 references]
https://hal-univ-perp.archives-ouvertes.fr/hal-01439207
Contributor : Dorian Miler <>
Submitted on : Wednesday, January 18, 2017 - 1:16:59 PM
Last modification on : Wednesday, October 14, 2020 - 3:58:31 AM
Long-term archiving on: : Wednesday, April 19, 2017 - 2:07:06 PM
Contributor : Dorian Miler <>
Submitted on : Wednesday, January 18, 2017 - 1:16:59 PM
Last modification on : Wednesday, October 14, 2020 - 3:58:31 AM
Long-term archiving on: : Wednesday, April 19, 2017 - 2:07:06 PM
File
journal.pone.0167755.pdf
Publisher files allowed on an open archive