2VPF
VASCULAR ENDOTHELIAL GROWTH FACTOR REFINED TO 1.93 ANGSTROMS RESOLUTION
Summary for 2VPF
Entry DOI | 10.2210/pdb2vpf/pdb |
Descriptor | VASCULAR ENDOTHELIAL GROWTH FACTOR (2 entities in total) |
Functional Keywords | growth factor, cystine knot, angiogenesis, vasculogenesis |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: P15692 |
Total number of polymer chains | 8 |
Total formula weight | 95589.44 |
Authors | Muller, Y.A.,De Vos, A.M. (deposition date: 1997-07-29, release date: 1998-07-29, Last modification date: 2024-10-16) |
Primary citation | Muller, Y.A.,Christinger, H.W.,Keyt, B.A.,de Vos, A.M. The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 A resolution: multiple copy flexibility and receptor binding. Structure, 5:1325-1338, 1997 Cited by PubMed Abstract: Vascular endothelial growth factor (VEGF) is an endothelial cell-specific angiogenic and vasculogenic mitogen. VEGF also plays a role in pathogenic vascularization which is associated with a number of clinical disorders, including cancer and rheumatoid arthritis. The development of VEGF antagonists, which prevent the interaction of VEGF with its receptor, may be important for the treatment of such disorders. VEGF is a homodimeric member of the cystine knot growth factor superfamily, showing greatest similarity to platelet-derived growth factor (PDGF). VEGF binds to two different tyrosine kinase receptors, kinase domain receptor (KDR) and Fms-like tyrosine kinase 1 (Flt-1), and a number of VEGF homologs are known with distinct patterns of specificity for these same receptors. The structure of VEGF will help define the location of the receptor-binding site, and shed light on the differences in specificity and cross-reactivity among the VEGF homologs. PubMed: 9351807DOI: 10.1016/S0969-2126(97)00284-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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