1RV6

Crystal Structure of PlGF in Complex with Domain 2 of VEGFR1

Summary for 1RV6

• Entry DOI: 10.2210/pdb1rv6/pdb
• Descriptor: placenta growth factor (PlGF), FLT1 protein, 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: plgf, vegf family, cystine knot, growth factor, ligand-receptor complex, specificity, hormone-growth factor-receptor complex, hormone/growth factor/receptor
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P49763; Isoform Flt1: Cell membrane; Single-pass type I membrane protein. Isoform sFlt1: Secreted: P17948
• Total number of polymer chains: 4
• Total formula weight: 46403.45

Authors

Christinger, H.W.,Fuh, G.,de Vos, A.M.,Wiesmann, C. (deposition date: 2003-12-12, release date: 2004-01-20, Last modification date: 2024-11-06)

Primary citation

Christinger, H.W.,Fuh, G.,de Vos, A.M.,Wiesmann, C.
The crystal structure of placental growth factor in complex with domain 2 of vascular endothelial growth factor receptor-1.
J.Biol.Chem., 279:10382-10388, 2004

PubMed Abstract: Placental growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family and plays an important role in pathological angiogenic events. PlGF exerts its biological activities through binding to VEGFR1, a receptor tyrosine kinase that consists of seven immunoglobulin-like domains in its extracellular portion. Here we report the crystal structure of PlGF bound to the second immunoglobulin-like domain of VEGFR1 at 2.5 A resolution and compare the complex to the closely related structure of VEGF bound to the same receptor domain. The two growth factors, PlGF and VEGF, share a sequence identity of approximately 50%. Despite this moderate sequence conservation, they bind to the same binding interface of VEGFR1 in a very similar fashion, suggesting that both growth factors could induce very similar if not identical signaling events.

PubMed: 14684734
DOI: 10.1074/jbc.M313237200

Experimental method

X-RAY DIFFRACTION (2.45 Å)