Additional supporting information may be found in the online version of this article.

AJMG_34199_sm_Suppl-Fig1.tif278KFig. 1: Mutation analysis of the FGFR3 mutation, c.1000G>A, p.Ala334Thr in the proband. A: Detection of the sequence variant in FGFR3 exon 8 (IIIc) by HRM. B: Electropherogram showing the identified FGFR3 p.Ala334Thr mutation.
AJMG_34199_sm_Suppl-Fig2.tif3284KFig. 2: Sequence homology and structural analysis of residue Alanine 334 in FGFR3. A: Alignment of FGFR3 and FGFR2 showing the conservation of Alanine 334 in FGFR3 with Alanine 337 in FGFR2 and the mutations identified at these amino acids. B: Conservation analysis of residue Alanine 334 in vertebrates; C: A ribbon representation of the X-ray coordinates provided by PDB ID#1RY7 of the FGFR3c-FGF1 complex (modified from [Olsen et al. 2004]). FGF1 is orange, FGFR3c IgIIc is green, IgIIIc is cyan, and the alternatively spliced C-terminal half of IgIIIc is purple. Localization of the Alanine 334 residue just before the βF loop of IgIIIc is indicated; D: A space filling representation of the region of interest surrounding Alanine 334 of the FGFR3c protein, with a similar orientation as in Supplemental Fig 2C. The brown residues are hydrophobic and the blue residues are hydrophilic. The mutated Alanine 334 residue is indicated in red. The βC′-βE loop is shown in green as a reference point.

Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.