Znfinger

Znfinger is a term occasionally used to refer to zinc finger motifs, a family of protein domains that bind nucleic acids and other molecules through a coordinated zinc ion. Zinc finger proteins play central roles in gene regulation and other cellular processes across many organisms.

These motifs are usually small, around 30 amino acids, and fold to form finger-like loops stabilized by a zinc ion coordinated by cysteine and histidine residues. The most studied type, the C2H2 zinc finger, consists of two cysteines and two histidines. In many proteins, multiple fingers are arranged in tandem to recognize longer DNA sequences, enabling sequence-specific binding. Synthetic zinc finger arrays have been engineered to target chosen genomic sites, an approach formerly used in zinc finger nucleases for genome editing and in gene regulation studies.

Although zinc finger technologies were once prominent in genome editing, the field has largely shifted toward CRISPR-based methods. Zinc finger domains remain important tools in molecular biology and are studied for therapeutic potential and basic science. The term Znfinger is not standard in scholarly use, but may appear as a stylized variant or shorthand for zinc finger in some texts. See also zinc finger, zinc finger protein, zinc finger nuclease (ZFN).