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• W2149594557 startingPage "413" @default.
• W2149594557 abstract "To elucidate the structural determinants governing specificity in fibroblast growth factor (FGF) signaling, we have determined the crystal structures of FGF1 and FGF2 complexed with the ligand binding domains (immunoglobulin-like domains 2 [D2] and 3 [D3]) of FGF receptor 1 (FGFR1) and FGFR2, respectively. Highly conserved FGF-D2 and FGF-linker (between D2-D3) interfaces define a general binding site for all FGF-FGFR complexes. Specificity is achieved through interactions between the N-terminal and central regions of FGFs and two loop regions in D3 that are subject to alternative splicing. These structures provide a molecular basis for FGF1 as a universal FGFR ligand and for modulation of FGF-FGFR specificity through primary sequence variations and alternative splicing." @default.
• W2149594557 created "2016-06-24" @default.
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• W2149594557 date "2000-05-01" @default.
• W2149594557 modified "2023-10-18" @default.
• W2149594557 title "Crystal Structures of Two FGF-FGFR Complexes Reveal the Determinants of Ligand-Receptor Specificity" @default.
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• W2149594557 doi "https://doi.org/10.1016/s0092-8674(00)80851-x" @default.
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• W2149594557 hasPublicationYear "2000" @default.
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