Characterization of the VEGF Binding Site on the Flt-1 Receptor
| Autor: | Ying Yu, M. T. Herley, J. D. Sato, R. G. Whitney |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Vascular Endothelial Growth Factor A
medicine.medical_treatment Restriction Mapping Endothelial Growth Factors Biochemistry Protein Structure Secondary Receptor tyrosine kinase chemistry.chemical_compound Cloning Molecular Receptor Lymphokines Membrane Glycoproteins biology Vascular Endothelial Growth Factors Cell adhesion molecule Recombinant Proteins Vascular endothelial growth factor embryonic structures cardiovascular system circulatory and respiratory physiology Recombinant Fusion Proteins Molecular Sequence Data Biophysics Proto-Oncogene Proteins Extracellular medicine Animals Humans Receptors Growth Factor Binding site Molecular Biology DNA Primers Glycoproteins Binding Sites Vascular Endothelial Growth Factor Receptor-1 Base Sequence Growth factor Membrane Proteins Receptor Protein-Tyrosine Kinases Kinase insert domain receptor Cell Biology equipment and supplies Molecular biology Rats Kinetics Receptors Vascular Endothelial Growth Factor Amino Acid Substitution chemistry Mutagenesis Site-Directed biology.protein sense organs Molecular Chaperones |
| Zdroj: | Biochemical and Biophysical Research Communications. 262:731-738 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1999.1282 |
| Popis: | The angiogenic growth factor VEGF binds to the receptor tyrosine kinases Flt-1 and KDR/Flk-1. Immunoglobulin (Ig)-like loop-2 of Flt-1 is involved in binding VEGF, but the contribution of other Flt-1 Ig-loops to VEGF binding remains unclear. We tested the ability of membrane-bound chimeras between the extracellular domain of Flt-1 and the cell adhesion molecule embigin to bind VEGF. VEGF bound as well to receptors containing Flt-1 loops 1-2 or 2-3 as it did to the entire Flt-1 extracellular domain. Chimeras containing only loop-2 of Flt-1 bound VEGF with 22-fold lower affinity. We conclude that high-affinity VEGF binding requires Ig-like loop-2 plus either loop-1 or loop-3. In addition, Flt-1 amino acid residues Arg-224 and Asp-231 were not essential for high-affinity binding of VEGF to membrane-bound Flt-1. |
| Databáze: | OpenAIRE |
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