Figure 3
Figure 3. Homology model of the EKLF-DNA complex. (A) Overall structure of the complex. DNA is shown as an orange molecular surface; protein is shown as a gray Cα cartoon. The amino terminus (Ala278) is labeled N; the carboxy terminus (Leu362) is labeled C. The side chains of mutated residues are highlighted as sticks with the carbon atoms of Arg328 and Arg331 colored green and cyan, respectively. (B) Close-up of the ZF2 domain highlighting protein-DNA interactions involving mutated residues. DNA is shown as sticks colored by atom type. Protein is displayed as in panel A. The bound water molecule is shown as a red sphere, and putative hydrogen bonds are shown as dashed yellow lines.

Homology model of the EKLF-DNA complex. (A) Overall structure of the complex. DNA is shown as an orange molecular surface; protein is shown as a gray Cα cartoon. The amino terminus (Ala278) is labeled N; the carboxy terminus (Leu362) is labeled C. The side chains of mutated residues are highlighted as sticks with the carbon atoms of Arg328 and Arg331 colored green and cyan, respectively. (B) Close-up of the ZF2 domain highlighting protein-DNA interactions involving mutated residues. DNA is shown as sticks colored by atom type. Protein is displayed as in panel A. The bound water molecule is shown as a red sphere, and putative hydrogen bonds are shown as dashed yellow lines.

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