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Plotnikov, AN, Hubbard, SR, Schlessinger, J and Mohammadi, M (2000) Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity. Cell 101:413-24


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.




Amino Acid Sequence; Fibroblast Growth Factor 1; Fibroblast Growth Factor 2/chemistry; Humans; Ligands; Molecular Sequence Data; Protein Binding; Protein Conformation; Receptors, Fibroblast Growth Factor/chemistry; Signal Transduction