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. 2018 Mar 1;29(5):610–621. doi: 10.1091/mbc.E17-06-0363

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© 2018 Silkworth et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.

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FIGURE 7: — Actin sequence variation near the FH2/actin interface. The Bni1 FH2 domain (blue)/ Oryctolagus cunniculus α-actin (gray) cocrystal structure (1Y64) provides a model for how actin sequence variation may determine formin interactions. Of the 11 nonconservative mutations between human β-actin and O. cunninculus α-actin, three residues (Thr5, Thr6, and Asn225) are within 6 Å of the FH2 domain. They are highlighted with red spheres. The N-terminal Thr residues are positioned to make van der Waals contacts with the FH2 linker region.