What protein contains a zinc finger domain?

Abstract. Zinc finger domains are one of the most common structural motifs in eukaryotic cells, which employ the motif in some of their most important proteins (including TFIIIA, CTCF, and ZiF268). These DNA binding proteins contain up to 37 zinc finger domains connected by flexible linker regions.

What do zinc finger domains bind to?

The zinc-finger domain is one of the most frequently utilized DNA-binding motif found in eukaryotic transcriptional factors. The binding of a zinc-finger domain to its target site juxtaposes three base pairs on DNA to a few amino acids in the α-helix structure.

How many amino acids long is a zinc finger domain?

30 amino acids long
Each zinc finger domain is 30 amino acids long and forms a ββα configuration, where individual amino acids in the α-helix interact with three successive nucleotide bases in the major groove of DNA (Figure 3.1(a)).

Is zinc finger domain tertiary?

Introduction. Zinc fingers (ZFs) are conventionally defined as short protein domains whose tertiary structure (or fold) is primarily stabilized by a structural zinc ion that serves as a surrogate for a strong hydrophobic core1,2,3,4.

What are zinc fingers and leucine zippers?

Leucine zippers are α-helices that contain a leucine residue every seventh amino acid. This motif is found in many eukaryotic transcription factors. Zinc fingers consist of 25-30 amino acids surrounding a single zinc atom, which is coordinated by two cysteines, which are very close to short α-helices.

What is zinc finger technology?

Zinc finger nucleases (ZFNs) are a class of engineered DNA-binding proteins that facilitate targeted editing of the genome by creating double-strand breaks in DNA at user-specified locations.

What are the other types of zinc finger domains?

The most common “fold groups” of zinc fingers are the Cys2His2-like (the “classic zinc finger”), treble clef, and zinc ribbon. Two ligands from a knuckle and two more from the c terminus of a helix. Two ligands from a knuckle and two more from a short helix or loop.

What are zinc finger and helix turn helix proteins?

Four distinct structural motifs have been proposed for the DNA-binding domains of eukaryotic transcriptional regulatory proteins; the helix-turn-helix, two kinds of zinc finger, and the leucine zipper.

Why is it called zinc finger?

Extended x-ray absorption fine structure confirmed the identity of the zinc ligands: two cysteines and two histidines. The DNA-binding loop formed by the coordination of these ligands by zinc were thought to resemble fingers, hence the name.