Turkish Journal of Biology




Fibroblast growth factor receptor (FGFR) is a cell membrane protein and a member of the tyrosine kinase family. It has extracellular domains that can be activated by ligand binding, followed by receptor dimerization. FGFR3 has 2 isoforms, 3b and 3c. The R248C mutation in FGFR3b leads to ligand independent receptor dimerization and results in different kinds of dermatological diseases such as seborrheic keratoses, acanthosis nigricans, and epidermal nevi. In order to prevent the increased cellular signaling caused by the R248C mutation, a pentapeptide ligand was designed that recognizes the mutation and binds to the receptor dimerization site. Molecular docking and steered molecular dynamics simulations were conducted, and binding free energy was calculated. The identified pentapeptide sequence appears to be a possible drug candidate for FGFR3b R248C mutation-related skin diseases.


FGFR3b, peptide drug, binding free energy, steered molecular dynamics

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