Download MendeleyCrystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor.
Wiesmann, C., Fuh, G., Christinger, H.W., Eigenbrot, C., Wells, J.A., de Vos, A.M.(1997) Cell 91: 695-704
- PubMed: 9393862
- DOI: https://doi.org/10.1016/s0092-8674(00)80456-0
- Primary Citation of Related Structures:
1FLT - 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.
Organizational Affiliation:
Genentech, Inc., Department of Protein Engineering, South San Francisco, California 94080, USA.
