Research Article

A Missense POU4F3 Variant Associated with Autosomal Dominant Midfrequency Hearing Loss Alters Subnuclear Localization and Transcriptional Capabilities

Figure 4

Evaluation of the transcriptional capabilities of wild-type (WT) and mutant (MUT) POU4F3 protein in its modulation of Prox1. 3D structural comparison of WT and MUT POU4F3 protein. (a) WT POU4F3 contains leu201 at the end of the first α-helix of the POU-specific domain. The distance between the side chains linking Leu201 to Glu256 and Leu201 to Val203 (dotted lines) is shown. (b) MUT POU4F3, with a Leu201 to Pro201 alteration, exhibited smaller side chains and different H-bond distances.
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