PMID: 9194163Apr 1, 1997Paper

Computer modelling of the receptor-binding domains of VEGF and PIGF

Protein Engineering
T P Walsh, G H Grant

Abstract

Models of the platelet-derived growth factor (PDGF)-like domains of vascular endothelial growth factor (VEGF) and placenta growth factor (PIGF) were built based on their homology to PDGF. These domains contain most of the determinants for receptor binding. The sequences of these proteins exhibit limited but significant homology to that of platelet-derived growth factor (PDGF), a member of the cystine knot growth factor family. The eight cysteine residues that are involved in intra- and interchain disulphide bonds are conserved. Two high affinity receptors for VEGF have been identified, only one of which binds PIGF. The models presented here are consistent with results that show that VEGF receptor binding is mediated by charged residues in the loops. A comparison of the models suggests that the difference in receptor-binding specificity between VEGF and PIGF may be due to differences in the distribution of positively charged residues and the exposure of hydrophobic residues in the loops.

Citations

Apr 20, 2004·Critical Reviews in Oncology/hematology·Amar BennasrounePierre Hubert
Dec 17, 2009·Acta Biomaterialia·C Katherine ChiangMilica Radisic
Apr 20, 2007·Biophysical Chemistry·Feilim Mac Gabhann, Aleksander S Popel
Apr 10, 2002·American Journal of Physiology. Cell Physiology·Michael Papetti, Ira M Herman
May 13, 1999·International Journal of Experimental Pathology·W P Leenders

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