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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.

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