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. Author manuscript; available in PMC: 2011 Mar 19.
Published in final edited form as: J Mol Biol. 2010 Jan 15;397(1):278–289. doi: 10.1016/j.jmb.2010.01.017

Figure 2.

Figure 2

Elf3 domain structure and sequence alignment. (A) Schematic diagram showing the domains of Elf3. (B) Structure-based sequence alignment of the DNA-bound Ets domains of Elf3, PDEF (1yo5), PU.1 (1pue), Sap1 (1k60), Elk1 (1dux), Ets1 (1k79), and GABPα (1awc). The secondary structure elements of Elf3 are indicated above the corresponding sequence. Helices are depicted by red rectangles and β strands as yellow arrows. The α3 helix terminates with a distorted 310 helix. Elf3 residues missing from the structure are highlighted in grey. Conserved residues are shown in red. The Elf3 residues interacting with DNA are underlined with brown color. Amino acid residues of Ets domains in direct contact with DNA bases are highlighted in cyan. (C) A stereoview of the three-dimensional alignment of Ets domains in the crystal structures of DNA-bound Elf3, PDEF, PU.1, Sap1, Elk1, Ets1, and GABPα. The α-carbon traces are shown as color-coded lines. The α-carbon position of every tenth amino acid residue of Elf3, starting from residue 280, is marked by a small circle.