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. 2011 Jun 15;14(12):2545–2579. doi: 10.1089/ars.2010.3445

FIG. 16.

FIG. 16.

(A) The C-terminal sequence alignment of the AIF-like proteins and (B) the x-ray structure of human AIF. (A) A DNA-binding helix-turn-helix motif predicted in D. discoideum is boxed. Residues corresponding to the 512Lys-Arg-Arg514 cluster in D. discoideum are also indicated. (B) The 595–605 peptide corresponding to the DNA-binding motif in D. discoideum is displayed in black. Instead of the basic cluster predicted to comprise the turn between helices in D. discoideum, human AIF has 594Asp-Gly-Glu596, which makes the surface more acidic and less suitable for DNA binding.