C2H2 zinc-finger motif presents in 3% of proteins that are encoded in the human genome, and has the abilities to recognize DNA, RNA and protein. With nearly 3 decades of efforts, the mechanisms of zinc-finger mediated biomolecule recognitions have been studied to various extents. Zinc-finger binds into the major groove of DNA double helix, establishes an one-to-one recognition format between DNA bases and certain amino acids in a zinc-finger, and achieves specificity based on DNA sequences. While RNA molecules show a large variety in their structures, zinc-finger recognizes RNA through the collected information of specially displayed bases and special backbone folding. Initial studies have been performed on zinc-finger mediated protein-protein interactions. Existing data indicate multiple recognition modes. The studies on molecular mechanism have supported the development of engineered zinc-fingers, which have been introduced into applications. For its wide existence, large functional diversity and potential in translational applications, zinc-finger deserves a systematic study in every aspect.
Amino Acid Sequence ; Animals ; Binding Sites ; DNA ; chemistry ; genetics ; Humans ; Ikaros Transcription Factor ; chemistry ; genetics ; Nuclear Proteins ; chemistry ; genetics ; Protein Binding ; Proteins ; chemistry ; genetics ; RNA, Ribosomal, 5S ; chemistry ; genetics ; Transcription Factor TFIIIA ; chemistry ; genetics ; Transcription Factors ; chemistry ; genetics ; Vesicular Transport Proteins ; chemistry ; genetics ; Zinc Fingers