Cys2His2 zinc finger protein family: classification, functions, and major members.
Cys2His2 (C2H2)-type zinc fingers are widespread DNA binding motifs in eukaryotic transcription factors. Zinc fingers are short protein motifs composed of two or three β-layers and one α-helix. Two cysteine and two histidine residues located in certain positions bind zinc to stabilize the structure. Four other amino acid residues localized in specific positions in the N-terminal region of the α-helix participate in DNA binding by interacting with hydrogen donors and acceptors exposed in the DNA major groove. The number of zinc fingers in a single protein can vary over a wide range, thus enabling variability of target DNA sequences. Besides DNA binding, zinc fingers can also provide protein-protein and RNA-protein interactions. For the most part, proteins containing the C2H2-type zinc fingers are trans regulators of gene expression that play an important role in cellular processes such as development, differentiation, and suppression of malignant cell transformation (oncosuppression).
Institute of Gene Biology, Russian Academy of Sciences, Moscow, 119334, Russia. info@genebiology.ru
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Razin
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Borunova
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Maksimenko
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Kantidze
D000818:Animals; D006801:Humans; D008969:Molecular Sequence Data; D005810:Multigene Family; D014157:Transcription Factors / Q000737:chemistry* / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D016335:Zinc Fingers
D014157:Transcription Factors