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  • Title: Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor.
    Author: Wiesmann C, Fuh G, Christinger HW, Eigenbrot C, Wells JA, de Vos AM.
    Journal: Cell; 1997 Nov 28; 91(5):695-704. PubMed ID: 9393862.
    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.
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