The Crystal Structure of Placental Growth Factor in Complex with Domain 2 of Vascular Endothelial Growth Factor Receptor-1

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 dom...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 2004-03, Vol.279 (11), p.10382-10388
Main Authors: Christinger, Hans W., Fuh, Germaine, de Vos, Abraham M., Wiesmann, Christian
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Circular Dichroism
Crystallography, X-Ray
Humans
Inhibitory Concentration 50
Ligands
Models, Biological
Models, Molecular
Molecular Sequence Data
Placenta Growth Factor
Pregnancy Proteins - chemistry
Protein Binding
Protein Folding
Protein Isoforms
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Vascular Endothelial Growth Factor Receptor-1 - chemistry
Vascular Endothelial Growth Factor Receptor-1 - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 Å 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 ∼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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M313237200