Zinc Finger Protein 767 (ZNF767)

Zinc Finger Protein 767 (ZNF767), Despite its name, it does not contain a canonical C2H2-type zinc-finger.A zinc finger protein is a DNA-binding protein domain consisting of zinc fingers ranging from two in the Drosophila regulator ADR1, the more common three in mammalian Sp1 up to nine in TFIIIA. They occur in nature as the part of transcription factors conferring DNA sequence specificity as the DNA-binding domain.

Zinc finger protein consists of anti-parallel hairpin motif. It consists of 2 beta strands, one alpha helix and a hairpin structure. The first Zn binds to Cys-3 of 1st beta strand, second Zn binds to Cys-6 that is present in the tight loop that separates the two beta strands. The other two Zn is coordinated to Cys 19 & 23 which are present in C-terminal half of the alpha helix. The hairpin is followed by alpha helix of about 3.5 turns.