[HTML][HTML] Identification of residues important both for primary receptor binding and specificity in fibroblast growth factor-7
Fibroblast growth factors (FGFs) mediate a multitude of physiological and pathological
processes by activating a family of tyrosine kinase receptors (FGFRs). Each FGFR binds to a
unique subset of FGFs and ligand binding specificity is essential in regulating FGF activity.
FGF-7 recognizes one FGFR isoform known as the FGFR2 IIIb isoform or keratinocyte
growth factor receptor (KGFR), whereas FGF-2 binds well to FGFR1, FGFR2, and FGFR4 but
interacts poorly with KGFR. Previously, mutations in FGF-2 identified a set of residues that …
processes by activating a family of tyrosine kinase receptors (FGFRs). Each FGFR binds to a
unique subset of FGFs and ligand binding specificity is essential in regulating FGF activity.
FGF-7 recognizes one FGFR isoform known as the FGFR2 IIIb isoform or keratinocyte
growth factor receptor (KGFR), whereas FGF-2 binds well to FGFR1, FGFR2, and FGFR4 but
interacts poorly with KGFR. Previously, mutations in FGF-2 identified a set of residues that …
