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. 2012 Jun 1;23(11):2057–2065. doi: 10.1091/mbc.E12-02-0120

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© 2012 Wang et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 6: — Modeling of wild-type (Glu-706) and IBM-3 mutant (Lys-706) myosin (A) In the pre–power stroke state (PDB: 1QVI), Glu-706 (green) is part of the SH1-SH2 helix of myosin (red). For orientation the relay helix is shown in blue (B) Substitution of the IBM-3 mutation (Lys-706, gray spheres) does not have a major effect on the pre–power stroke structure (C) The wild-type SH1 helix containing Glu-706 (green spheres) melts during the power stroke, as shown here (red) in the post–power stroke state (PDB: 1KK8). (D) The IBM-3 mutation (Lys-706; gray spheres) is predicted to alter the orientation of the melted helix (red) in the post–power stroke state, bringing it in contact (2.8 Å) with Asp-98 (light blue spheres) in the N-terminal region. This new charge-based interaction may prevent reformation of the SH1 helical region of the SH1-SH2 helix after ATP binding.