1rv6

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.

The crystal structure of placental growth factor in complex with domain 2 of vascular endothelial growth factor receptor-1., Christinger HW, Fuh G, de Vos AM, Wiesmann C, J Biol Chem. 2004 Mar 12;279(11):10382-8. Epub 2003 Dec 18. PMID:14684734

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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OCA, David Canner

Categories: Homo sapiens | Christinger, H W. | Fuh, G. | Vos, A M.de. | Wiesmann, C. | Cystine knot | Growth factor | Ligand-receptor complex | Plgf | Specificity | Vegf family