In: Biology
A zinc finger is a structural motif of protein. It is characterised by the co-ordination of one or more zinc ions. The name zinc finger comes from finger like appearance of transcription factor IIIA which was discovered from Xenopus sp. The structure has multiple finger like protrusions which makes contact with the target molecule. The finger like folds are stabilised by salt bridges. They co-ordinate zinc ions with a combination of cysteine and histidine residues. The zinc finger can be classified into fold groups based on the shape of backbone of protein in the domain. The types include classic zinc finger, treble clef and zinc ribbon. In the classic zinc finger motif, two of the ligands form a knuckle while the other two form the C terminus of the helix. In treble clef, the structure is more or less similar to classic zinc finger except for the fact that the 3rd and the 4th ligands form the N terminus of the helix. In zinc ribbon, two ligands forms two knuckles.