Zinc finger protein
Encyclopedia
A zinc finger protein is a DNA-binding protein domain consisting of zinc finger
Zinc finger
Zinc fingers are small protein structural motifs that can coordinate one or more zinc ions to help stabilize their folds. They can be classified into several different structural families and typically function as interaction modules that bind DNA, RNA, proteins, or small molecules...

s ranging from two in the Drosophila
Drosophila
Drosophila is a genus of small flies, belonging to the family Drosophilidae, whose members are often called "fruit flies" or more appropriately pomace flies, vinegar flies, or wine flies, a reference to the characteristic of many species to linger around overripe or rotting fruit...

regulator ADR1, the more common three in mammalian Sp1 up to nine in TFIIIA. They occur in nature as the part of transcription factor
Transcription factor
In molecular biology and genetics, a transcription factor is a protein that binds to specific DNA sequences, thereby controlling the flow of genetic information from DNA to mRNA...

s conferring DNA sequence specificity as the DNA-binding domain
DNA-binding domain
A DNA-binding domain is an independently folded protein domain that contains at least one motif that recognizes double- or single-stranded DNA. A DBD can recognize a specific DNA sequence or have a general affinity to DNA...

.

They have also found use in protein engineering
Protein engineering
Protein engineering is the process of developing useful or valuable proteins. It is a young discipline, with much research taking place into the understanding of protein folding and recognition for protein design principles....

 due to their modularity and have prospects as components of tools for use in therapeutic gene modulation
Therapeutic gene modulation
Therapeutic gene modulation refers the practice of altering the expression of a gene at one of various stages, with a view to alleviate some form of ailment...

 and zinc finger nucleases.

Structure

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. The binding of Zn at the last two positions mentioned causes distortion in alpha helix between these positions to form a 3-10 complex in which H bonding occurs between 1st and 3rd amino acid instead of 1-4 amino acid bonding. Zn in buried in the interior of the protein and is necessary for the formation of a stable finger structure in aqueous solution. The zinc does not interact with DNA.

See also

  • Zinc finger chimera
    Zinc finger chimera
    Zinc finger protein chimera are chimeric proteins composed of a DNA-binding zinc finger protein domain and another domain through which the protein exerts its effect...

     - an exploitation of zinc fingers in protein engineering
    Protein engineering
    Protein engineering is the process of developing useful or valuable proteins. It is a young discipline, with much research taking place into the understanding of protein folding and recognition for protein design principles....

  • Zinc finger nuclease
    Zinc finger nuclease
    Zinc-finger nucleases are artificial restriction enzymes generated by fusing a zinc finger DNA-binding domain to a DNA-cleavage domain. Zinc finger domains can be engineered to target desired DNA sequences and this enables zinc-finger nucleases to target unique sequences within complex genomes...

  • Zinc finger inhibitor
    Zinc finger inhibitor
    Zinc finger inhibition is the process by which the synthesis of zinc fingers is blocked. Zinc finger inhibitors have been tested for their efficacy in treating AIDS and HIV....

  • Zinc finger
    Zinc finger
    Zinc fingers are small protein structural motifs that can coordinate one or more zinc ions to help stabilize their folds. They can be classified into several different structural families and typically function as interaction modules that bind DNA, RNA, proteins, or small molecules...

     -
  • DNA-binding domains
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