The crystal structure of placental growth factor in complex with domain 2 of vascular endothelial growth factor receptor-1
| Autor: | Germaine Fuh, Christian Wiesmann, Abraham M. de Vos, H.W. Christinger |
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| Rok vydání: | 2003 |
| Předmět: |
Placental growth factor
Models Molecular Protein Folding Molecular Sequence Data Plasma protein binding Pregnancy Proteins Crystallography X-Ray Ligands Biochemistry Models Biological Receptor tyrosine kinase Protein Structure Secondary chemistry.chemical_compound Inhibitory Concentration 50 Protein structure Extracellular Humans Protein Isoforms Amino Acid Sequence Receptor Molecular Biology Peptide sequence Placenta Growth Factor Vascular Endothelial Growth Factor Receptor-1 biology Sequence Homology Amino Acid Circular Dichroism Cell Biology Cell biology Protein Structure Tertiary Vascular endothelial growth factor chemistry Immunology biology.protein Protein Binding |
| Zdroj: | The Journal of biological chemistry. 279(11) |
| ISSN: | 0021-9258 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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