Summary
PDB 1FLT deposited: 1997-11-20 modified: 2012-05-02
Title VEGF IN COMPLEX WITH DOMAIN 2 OF THE FLT-1 RECEPTOR
Authors Christinger, H.W., de Vos, A.M., Eigenbrot, C., Fuh, G., Wells, J.A., Wiesmann, C.
Method X-RAY DIFFRACTION
Structure factors resolution 1.7 rfactor 0.198 rfree 0.261
DPI 0.34 theoretical min: 0.14
Citations

"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."

Cell(Cambridge,Mass.) 1997 Nov; 91(5):695-704 doi:10.1016/S0092-8674(00)80456-0

Cross References
Database source Identifier Description
PubMed 9393862 CELLB5
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1FLT/1 1FLT 1 tetramer 0 4 0 3464
1FLT/2 1FLT 2 octamer 0 8 0 6928