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4CL7

Crystal structure of VEGFR-1 domain 2 in presence of Cobalt

Summary for 4CL7
Entry DOI10.2210/pdb4cl7/pdb
Related4CKV
DescriptorVASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1, COBALT (II) ION, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordsreceptor, metal-binding
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains4
Total formula weight43827.24
Authors
Primary citationGaucher, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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건을2024-10-30부터공개중

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