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. Author manuscript; available in PMC: 2010 Nov 14.
Published in final edited form as: Nat Genet. 2009 Dec 20;42(1):72–76. doi: 10.1038/ng.505

Figure 2. INF2 mutations.

Figure 2

a. Disease-segregating INF2 mutations shown aligned with wild-type INF2 protein sequence from humans, chimpanzee, mouse, rat, opossum, and zebrafish. All of these disease mutations occur in evolutionarily conserved residues within the DID.

b. Schematic showing INF2 protein domain structure and location of mutations.

c, d, and e: Model of mouse INF2 amino acids 1–330, based on the structure of mDia1 (1). Mutated residues are shown in red, and residues important for the interaction with DAD are shown in blue.

c. View of mDia1 showing the positions of A13 and R218 (red). Residues important for the direct interaction with DAD are shown in blue, including R106 (corresponding to K213 in mDia1), N110 (corresponding to N217 in mDia1), A149 (corresponding to A256 in mDia1), and I152 (corresponding to I259 in mDia1). Based on the crystal structure of the mDia1 DID/DAD complex (reference 22), the alpha helical INF2 DAD is predicted to lie in the pocket containing these residues, with its N-terminus (D974) contacting R106 and N110, and L986 contacting A149 and I152. In this model, we predict that R218 would contact residues C-terminal to L986.

d. Close-up of the portion of the INF2 region predicted to interact with the DAD.

e. 180 degree rotation of the structure shown in F1, showing L42, S186, and E220.