zincfingerproteiner
Zinc finger proteins are a large superfamily of proteins characterized by the presence of zinc finger motifs, small structural modules stabilized by a bound zinc ion. The most common motif, the C2H2 zinc finger, consists of about 30 amino acids that coordinate a Zn2+ ion through two cysteine residues and two histidine residues, forming a compact fold that presents a DNA-binding surface. Proteins may contain one or many fingers in tandem, enabling recognition of longer DNA sequences.
Zinc finger domains can bind DNA, RNA, or other proteins. In DNA-binding zinc finger proteins, arrays of
Applications and engineering: The concept of zinc finger nucleases (ZFNs) combines engineered zinc finger arrays with
Discovery and evolution: The zinc finger motif was identified in the 1980s in transcription factors such as