What is C2H2 zinc finger?

What is C2H2 zinc finger?

C2H2 zinc fingers (Cys2-His2) represent one of the most common domains found in the TFs of higher eukaryotes. The classical C2H2 domain of 28–30 aa includes a β-hairpin (antiparallel β-sheet consisting of two β-strands), followed by an α-helix, which form a left-handed ββα structure (Fig. 1A).

What type of protein is zinc finger?

Zinc finger protein (ZFP) is a common DNA binding domain found in many transcription factors. It consists of ∼30 amino acids that may recognize three base pairs of DNA.

What does zinc finger protein do?

Zinc finger proteins are among the most abundant proteins in eukaryotic genomes. Their functions are extraordinarily diverse and include DNA recognition, RNA packaging, transcriptional activation, regulation of apoptosis, protein folding and assembly, and lipid binding.

What is the structural fold of the C2H2 zinc finger protein?

The Cys2His2-like fold group (C2H2) is by far the best-characterized class of zinc fingers, and is common in mammalian transcription factors. Such domains adopt a simple ββα fold and have the amino acid sequence motif: X2-Cys-X2,4-Cys-X12-His-X3,4,5-His.

How does zinc finger work?

As you can see from these structures, the string of zinc fingers curls along the DNA or RNA strands, binding in the grooves and extending amino acids inwards to read the bases. A single zinc finger does not bind very tightly and can only recognize 2 or 3 base pairs.

How do zinc finger nucleases work?

Zinc-finger nucleases usually operate by involving two DNA binding proteins, which contain 3–6 zinc fingers and FokI endonuclease to dimerize to cleave the double-strand DNA. These two proteins identified two DNA sequences and connected the two zinc-finger proteins to specific sequences.

Do proteins contain zinc?

Zn proteins are therefore found among all 6 Enzyme Commission (EC) classes and recent estimates suggest that close to 10% of all eukaryotic proteins are Zn-dependent [26,27].

What causes zinc deficiency?

Zinc deficiency is characterized by growth retardation, loss of appetite, and impaired immune function. In more severe cases, zinc deficiency causes hair loss, diarrhea, delayed sexual maturation, impotence, hypogonadism in males, and eye and skin lesions [2,8,25,26].

What does a zinc finger domain do?

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.

What do zinc fingers interact with?

Zinc-finger proteins (ZNFs) are one of the most abundant groups of proteins and have a wide range of molecular functions. Given the wide variety of zinc-finger domains, ZNFs are able to interact with DNA, RNA, PAR (poly-ADP-ribose) and other proteins.

How does zinc finger interact with DNA?

Zinc fingers bind in the major groove of the DNA, wrapping around the strands, with specificity conferred by side chains of several amino acid on the α helices. Some zinc finger proteins undergo homodimerization by hydrophobic interactions or by finger-finger binding and reinforce the specific binding to DNA.

Is the C2H2 zinc finger domain a stable structure?

Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. This entry represents the classical C2H2 zinc finger domain. 1 .^ Three classes of C2H2 zinc finger proteins.

What are the protrusions of a zinc finger domain?

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule.

Where is the C2H2 zinc finger degrome targeted?

Science. 2018 Nov 2;362 (6414):eaat0572. doi: 10.1126/science.aat0572. 1 Broad Institute of Harvard and MIT, Cambridge, MA 02142, USA. 2 Brigham and Women’s Hospital, Division of Hematology, Harvard Medical School, Boston, MA 02115, USA. 3 Friedrich Miescher Institute for Biomedical Research, 4058 Basel, Switzerland.

Which is the first type of zinc finger?

C2H2-type (classical) zinc fingers (Znf) were the first class to be characterised. They contain a short beta hairpin and an alpha helix (beta/beta/alpha structure), where a single zinc atom is held in place by Cys(2)His(2) (C2H2) residues in a tetrahedral array.