1FLT
VEGF IN COMPLEX WITH DOMAIN 2 OF THE FLT-1 RECEPTOR
Summary for 1FLT
| Entry DOI | 10.2210/pdb1flt/pdb |
| Descriptor | VASCULAR ENDOTHELIAL GROWTH FACTOR, FMS-LIKE TYROSINE KINASE 1 (3 entities in total) |
| Functional Keywords | complex (growth factor-transferase), flt-1 receptor, cystine knot, glycoprotein, immunoglobulin-like domain transferase, complex (growth factor-transferase) complex, complex (growth factor/transferase) |
| Biological source | Homo sapiens (human) More |
| Cellular location | Secreted: P15692 Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 3: Secreted. Isoform 4: Secreted. Isoform 5: Cytoplasm (Potential). Isoform 6: Cytoplasm (Potential). Isoform 7: Cytoplasm (Potential): P17948 |
| Total number of polymer chains | 4 |
| Total formula weight | 44835.82 |
| Authors | Wiesmann, C.,De Vos, A.M. (deposition date: 1997-11-20, release date: 1999-01-13, Last modification date: 2024-10-30) |
| Primary citation | Wiesmann, C.,Fuh, G.,Christinger, H.W.,Eigenbrot, C.,Wells, J.A.,de Vos, A.M. Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor. Cell(Cambridge,Mass.), 91:695-704, 1997 Cited by PubMed Abstract: Vascular endothelial growth factor (VEGF) is a homodimeric hormone that induces proliferation of endothelial cells through binding to the kinase domain receptor and the Fms-like tyrosine kinase receptor (Flt-1), the extracellular portions of which consist of seven immunoglobulin domains. We show that the second and third domains of Flt-1 are necessary and sufficient for binding VEGF with near-native affinity, and that domain 2 alone binds only 60-fold less tightly than wild-type. The crystal structure of the complex between VEGF and the second domain of Flt-1 shows domain 2 in a predominantly hydrophobic interaction with the "poles" of the VEGF dimer. Based on this structure and on mutational data, we present a model of VEGF bound to the first four domains of Flt-1. PubMed: 9393862DOI: 10.1016/S0092-8674(00)80456-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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