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Craniosynostosis, which affects approximately 1 in 2000 children, is the result of the abnormal development and/or premature fusion of the cranial sutures. Studies of mutations in patients with craniosynostosis have shown that the family of fibroblast growth factor receptor genes are extremely important in the correct formation of the skull, and digits. Mutations in the third immunoglobulin domain of fibroblast growth factor receptor 2 (FGFR2), in part of the molecule corresponding to a tissue specific isoform (IIIc), can cause both Crouzon and Pfeiffer syndromes. Two specific mutations in the linking region between the second and third immunoglobulin domains of FGFR2 occur in Apert syndrome. We present here mutations associated with the Crouzon syndrome, also in the third immunoglobulin domain but in an upstream exon. This exon is expressed in both tissue isoforms. Five different mutations were detected in 11 unrelated individuals. A cysteine to phenylalanine change was found in six individuals. This cysteine forms half of the disulphide bridge maintaining the secondary structure of the immunoglobulin domain. The first deletion within an FGFR gene is reported. Together with mutations in exon IIIc these account for 25 mutations out of 40 Crouzon patients studied in our combined series (5).


Journal article


Hum Mol Genet

Publication Date





1077 - 1082


Amino Acid Sequence, Base Sequence, Craniofacial Dysostosis, DNA, DNA Mutational Analysis, Exons, Female, Humans, Male, Molecular Sequence Data, Mutation, Receptor Protein-Tyrosine Kinases, Receptor, Fibroblast Growth Factor, Type 2, Receptors, Fibroblast Growth Factor, Sequence Homology, Amino Acid