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. 2016 Mar 17;98(4):627–642. doi: 10.1016/j.ajhg.2016.02.008

Figure 4.

Figure 4

Identification of Missense Mutations in GTF2E2 in Affected Children TTD379BE and TTD28PV

(A) Electropherograms showing the change identified in GTF2E2 in TTD379BE and his unaffected father and mother but not in the unaffected brother.

(B) Electropherograms showing the change identified in GTF2E2 (GenBank: NM_002095.4, NC_000008.10) in TTD28PV and unaffected father, mother, and sister but not in the unaffected brother. For cDNA numbering, +1 corresponds to the A of the ATG translation initiation codon in the reference sequence.

(C) Conservation of amino acids Ala150 and Asp187 in multiple protein sequence alignment of TFIIEβ regions in 13 species (from HomoloGene: 37573).

(D) Structural location of amino acid changes in TFIIEβ protein resulting from GTF2E2 homozygous missense mutations in TTD-affected individuals. Each winged-helix (WH) domain consists of three helices (cylinders) and a beta-hairpin (two strands). The protein is colored from N to C terminus from blue (WH1 domain), blue-green (WH2 domain), to red (C terminus). The altered amino acids (p.Ala150Pro and p.Asp187Tyr) are 14 Å apart on different surfaces of wing helix 2 (WH2) region of the TFIIEβ protein. The p.Ala150Pro change will destabilize the long alpha helix and cause it to bend or locally unfold (W. Yang, personal communication).