Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity.

By A. Plotnikov, S. Hubbard, Joseph Schlessinger, M. Mohammadi. 2000

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Structural basis for fibroblast growth factor receptor activation. (2005, background): “Indeed, comparison of the crystal structure of FGF2 in complex with FGFR2c [129] and FGF10 in complex with FGFR2b [124] illustrates that in each structure the bC0–bE loop makes specific contacts with b4 strand and N-terminus of FGF.”
FGF signaling pathways in endochondral and intramembranous bone development and human genetic disease. (2002, background): “However, the mutant receptor in AS has lost ligand-binding specificity and thus can be activated by inappropriate ligands (Plotnikov et al. 2000; Yu et al. 2000; Ibrahimi et al. 2001; Yu and Ornitz 2001).”
Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization. (2000, background): “…to FGF stimulation (Ornitz Joseph Schlessinger,*‖ Alexander N. Plotnikov,*‖ Omar A. Ibrahimi,* Anna V. Eliseenkova,* Brian K. Yeh,* Avner Yayon,† Robert J. Linhardt,‡ and Moosa Mohammadi*§ *Department of Pharmacology New York University School of Medicine et al., 1996; Plotnikov et al., 2000).”