Abstract
Fibroblast growth factor 3 (FGFR3), a member of the receptor tyrosine kinase (RTK) family, is an important mediator of cellular signaling. Signal transduction is achieved by receptor dimerization, phosphorylation and stimulation of downstream signaling cascades. Single amino acid mutations can affect the signaling and lead to overactivation and pathologies. Ala391Glu is one FGFR3 pathogenic mutation, causing crouzon syndrome with acanthosis nigricans. We investigate the effect of this mutation in the context of full length FGFR3 in 293T cell, and in the presence of the ligand acidic fibroblast growth factor (FGF1). By fitting the Western blot data to a thermodynamic model describing an apparent equilibrium between inactive monomers and active dimers, we find that the Ala391Glu mutation increases the activation prospensity by about ‐2 kcal/mole.
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