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. 2015 May 15;26(10):1875–1886. doi: 10.1091/mbc.E14-11-1558

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© 2015 Yoo, Roth-Johnson, 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 2: — Structural analysis of capu missense mutations. (A) Domain organization of Capu (1059 amino acids) and schematic of the C-terminal construct used in this study (CapuCT): CID, Capu inhibitory domain; FH1, formin homology 1; FH2, formin homology 2 (residues 554–1028); T, tail. Stars indicate the mutations, which are all located within Capu's FH2 domain. Residues are colored as in other images. (B) Locations of mutated residues within the FH2 domain based on a Capu homology model. The model was generated from the hDAAM1 crystal structure (Protein Data Bank # 2J1D; Lu et al., 2007) using SWISS-MODEL (Arnold et al., 2006). (C) Size exclusion chromatography of all mutants compared with wild-type CapuCT (dimer) and CapuCT-W600A (monomer) controls. The dashed purples line is the elution pattern from running the CapuCT-H977Y dimer peak a second time on the column.