FGFR3c P250R mutant binds to ligand with enhanced affinity Authored: Rothfels, K, 2012-02-09 Edited: Rothfels, K, 2012-05-16 FGFR3 P350R is associated with the development of Muenke syndrome, a milder craniosynostotic condition than Apert Syndrome (Bellus, 1996; Reardon, 1997). This mutation, which falls in the highly conserved Ser-Pro dipeptide in the IgII-IgIII linker, has been shown to increase the affinity of the receptor for its natural ligands, particularly for FGF9 (Ibrahimi, 2004a), without expanding the ligand-binding range of the receptor. This difference, compared to the paralogous FGFR2 S252W and P253R mutations, which bind an expanded range of ligands, is thought to account for the milder phenotype of Muenke Syndrome (Yu, 2000; Ibrahimi, 2004a, b). Pubmed11121055 Pubmed14613973 Pubmed15282208 Pubmed8841188 Pubmed9279753 Reactome Database ID Release 432012074 Reactome, http://www.reactome.org ReactomeREACT_121378 Reviewed: Ezzat, S, 2012-05-15 has a Stoichiometric coefficient of 2 FGFR3c P250R mutant dimer bound to FGF FGFR3c-binding FGFs