Summary
PDB 1RV6 deposited: 2003-12-12 modified: 2011-07-13
Title Crystal Structure of PlGF in Complex with Domain 2 of VEGFR1
Authors Christinger, H.W., de Vos, A.M., Fuh, G., Wiesmann, C.
Method X-RAY DIFFRACTION
Structure factors resolution 2.45 rfactor 0.19367 rfree 0.26022
DPI 0.80 theoretical min: 0.35
Citations

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.

J.Biol.Chem. 2004 Mar; 279(11):10382-10388 doi:10.1074/jbc.M313237200

Cross References
Database source Identifier Description
PubMed 14684734 JBCHA3
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1RV6/1 1RV6 1 tetramer 0 4 1 3034