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. Author manuscript; available in PMC: 2019 Nov 1.
Published in final edited form as: Am J Med Genet A. 2018 Sep 14;176(11):2404–2418. doi: 10.1002/ajmg.a.40482

Fig.6: Predicted and apparent destabilization of DDX11 protein by R378P mutation.

Fig.6:

(A) Alignment of secondary structure of DDX11 based on Thermoplasma acidophillum (Ta) XPD as a template using Phre2 protein fold recognition server. Region of secondary structure spanning R378 amino acid (in Block) is shown. (B) Predicted modeled structure of DDX11 protein. Human DDX11 protein was modeled by Phyre2 protein fold recognition server. Structure is based on homology modeling using TaXPD (Kuper et al., 2012). Arg-378 with side chain (ball and stick) is shown and indicated in edged red surface. (C) Effect of Proteasome inhibitor MG132 on the expression of DDX11 proteins. 293T cells transfected with DDX11-WT, DDX11-R378P#1 (R378P#1), or DDX11-R378P#2 (R378P#2) were either treated with MG132 (10 μM) or DMSO used as a not treated (NT) for 14 h. Cell lysates were prepared and resolved by SDS-PAGE, followed by Western blot detection with FLAG antibody. Actin was used as a loading control.