Crystal structure of the Cys2His2-type zinc finger domain of human DPF2

DPF2 is an evolutionary highly conserved member of the d4-protein family characterized by an N-terminal 2/3 domain, a C2H2-type zinc finger (ZF), and a C-terminal tandem PHD zinc finger. DPF2 is identified as a transcription factor and may be related with some cancers in human. Here, we report the crystal structure of the C2H2-type zinc finger domain of human DPF2 with a canonical C2H2 fold, which contains two beta strands and one alpha helix. Several conserved residues, including Lys207, Lys216 and Arg217, constitute a positively charged surface in C2H2 domain, which implicates that it has the potential to bind DNA. The side chains of the residues Y209, C211, C214, K216, Y218, L224, H227 and H232 form the hydrophobic core of C2H2 domain, which indicates a potential-binding surface in the human DPF2.

► This is the first structural information of human DPF2.
► The structure of the protein with a C2H2 fold, which contains two beta strands and one alpha helix.
► Several conserved residues of the protein, constitute a DNA-binding surface of human DPF2.
► The side chains of the residues form the hydrophobic core of C2H2 domain.