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Biophysical Studiesof the InducedDimerization of HumanVEGF Receptor 1Binding Domain byDivalent MetalsCompeting with VEGF-A Jean‐François GaucherMarie Reille‐SeroussiNathalie Gagey‐Eilstein2016 год

Biophysical Studies of the Induced Dimerization of Human VEGF Receptor 1 Binding Domain by Divalent Metals Competing with VEGF-A
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Аннотация: 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 Zn2+, Co2+ or Cu2+ 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 Co2+, Cd2+ or Cu2+. 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.
Год издания: 2016
Авторы: Jean‐François Gaucher, Marie Reille‐Seroussi, Nathalie Gagey‐Eilstein, Sylvain Broussy, Pascale Coric, Bili Seijo, Marie‐Bernard Lascombe, Benoît Gautier, Wang‐Qing Liu, Florent Huguenot, Nicolas Inguimbert, Serge Bouaziz, Michel Vidal, Isabelle Broutin
Издательство: Public Library of Science
Источник: PLoS ONE
Ключевые слова: Angiogenesis and VEGF in Cancer, Cell Adhesion Molecules Research, Inflammatory mediators and NSAID effects
Другие ссылки: PLoS ONE (PDF)
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