Zinc-finger DNA binding protein (ZNF)

Zinc-finger DNA binding proteins contain structural motifs called zinc fingers, typically stabilized by the coordination of zinc ions with cysteine and histidine residues. The classical C2H2 zinc finger motif is the most common DNA-binding domain in eukaryotic transcription factors. These proteins bind DNA, often in a sequence-specific manner, and regulate gene expression, chromatin structure, and many other cellular processes. The protein family is highly versatile—members can also bind RNA, other proteins, and lipids, influencing cell cycle, apoptosis, differentiation, and stress responses. Dysregulation of zinc-finger DNA binding proteins is implicated in diverse diseases, prominently cancer, and their domains form the basis of therapeutically important gene editing tools such as zinc finger nucleases.

Other names

Zinc finger proteinZNFC2H2 zinc finger proteinDNA-binding zinc finger proteinzinc finger transcription factor

Gene editing via engineered zinc finger nucleases (ZFNs): targeted DNA cleavage for mutagenesis or gene correction Modulation of transcription factor activity (regulating gene expression at the DNA level)