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. Author manuscript; available in PMC: 2015 Sep 1.
Published in final edited form as: Hum Mutat. 2014 Jul 17;35(9):1101–1113. doi: 10.1002/humu.22602

Figure 1. Predicted structural features of torsinA variants, their dimerization and molecular dynamics.

Figure 1

(A) Overall organization and sequence variations in torsinA (SS = signal sequence; Hypb = hydrophobic domain; AAA+ domain; and C-terminal domain). (B) Overall, structure of human torsinA. AAA+ domain is composed by 11 alpha helices (light green) and 5 beta strands (dark green), and the C-terminal domain is composed by 3 alpha helices, where the alpha 13 and 14 are colored in light blue and alpha 15 is in dark blue. ATP molecule is represented by its chemical structure (orange, purple and yellow). (C) Location of each of the four torsinA mutations studied is superimposed on the torsinAwt model. In torsinAwt a.a. carbons are colored in orange and the mutants are colored in yellow. Image generated with PyMol. (D) Lysates of BE(2)C cells (30 µg) expressing torsinAwt or torsinA variants: torsinAΔE, torsinAR288Q, and torsinAF205I were electrophoresed under non-reducing and reducing (200 mM DTT) conditions and gels immunoblotted with antibodies to torsinA or beta-actin. (E) Quantification of the band intensity of 75 kDa "dimers" in non-reducing conditions for torsinAwt, torsinAΔE, torsinAR288Q, and torsinAF205I relative to levels of beta-actin (ANOVA post-hoc Dunnett's t-test *p<0.05; **p<0.01; ***p<0.001; n=5). (F) Molecular dynamics analyses of torsinAwt and variants.