5ABD

CRYSTAL STRUCTURE OF VEGFR-1 DOMAIN 2 IN PRESENCE OF CU

Summary for 5ABD

• Entry DOI: 10.2210/pdb5abd/pdb
• Descriptor: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1, SODIUM ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: signaling protein, vegf, receptor
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 3
• Total formula weight: 33275.82

Authors

Gaucher, J.-F.,Lascombe, M.-B.,Reille-Seroussi, M.,Gagey-Eilstein, N.,Broussy, S.,Coric, P.,Seijo, B.,Gautier, B.,Liu, W.-Q.,Huguenot, F.,Inguimbert, N.,Bouaziz, S.,Vidal, M.,Broutin, I. (deposition date: 2015-08-05, release date: 2016-09-28, Last modification date: 2024-11-06)

Primary citation

Gaucher, J.-F.,Reille-Seroussi, M.,Gagey-Eilstein, N.,Broussy, S.,Coric, P.,Seijo, B.,Lascombe, M.-B.,Gautier, B.,Liu, W.-Q.,Huguenot, F.,Inguimbert, N.,Bouaziz, S.,Vidal, M.,Broutin, I.
Biophysical Studies of the Induced Dimerization of Human Vegf R Receptor 1 Binding Domain by Divalent Metals Competing with Vegf-A
Plos One, 11:67755-, 2016

PubMed 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 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.

PubMed: 27942001
DOI: 10.1371/JOURNAL.PONE.0167755

Experimental method

X-RAY DIFFRACTION (1.995 Å)