Small structural protein motif found mostly in transcriptional proteins
"ZFP" redirects here. For a consultancy firm, see Zuhair Fayez Partnership.
Cartoon representation of the Cys2His2 zinc finger motif, consisting of an α helix and an antiparallel β sheet. The zinc ion (green) is coordinated by two histidine residues and two cysteine residues.Cartoon representation of the protein Zif268 (blue) containing three zinc fingers in complex with DNA (orange). The coordinating amino acid residues and zinc ions (green) are highlighted.
A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn2+) which stabilizes the fold. It was originally coined to describe the finger-like appearance of a hypothesized structure from the African clawed frog (Xenopus laevis) transcription factor IIIA. However, it has been found to encompass a wide variety of differing protein structures in eukaryotic cells.[1]Xenopus laevis TFIIIA was originally demonstrated to contain zinc and require the metal for function in 1983, the first such reported zinc requirement for a gene regulatory protein[2][3] followed soon thereafter by the Krüppel factor in Drosophila.[4] It often appears as a metal-binding domain in multi-domain proteins.[3]
Proteins that contain zinc fingers (zinc finger proteins) are classified into several different structural families. Unlike many other clearly defined supersecondary structures such as Greek keys or β hairpins, there are a number of types of zinc fingers, each with a unique three-dimensional architecture. A particular zinc finger protein's class is determined by this three-dimensional structure, but it can also be recognized based on the primary structure of the protein or the identity of the ligands coordinating the zinc ion. In spite of the large variety of these proteins, however, the vast majority typically function as interaction modules that bind DNA, RNA, proteins, or other small, useful molecules, and variations in structure serve primarily to alter the binding specificity of a particular protein.
Since their original discovery and the elucidation of their structure, these interaction modules have proven ubiquitous in the biological world and may be found in 3% of the genes of the human genome.[5] In addition, zinc fingers have become extremely useful in various therapeutic and research capacities. Engineering zinc fingers to have an affinity for a specific sequence is an area of active research, and zinc finger nucleases and zinc finger transcription factors are two of the most important applications of this to be realized to date.
^Klug A, Rhodes D (1987). "Zinc fingers: a novel protein fold for nucleic acid recognition". Cold Spring Harbor Symposia on Quantitative Biology. 52: 473–82. doi:10.1101/sqb.1987.052.01.054. PMID 3135979.
^Hanas JS, Hazuda DJ, Bogenhagen DF, Wu FY, Wu CW (December 1983). "Xenopus transcription factor A requires zinc for binding to the 5 S RNA gene". The Journal of Biological Chemistry. 258 (23): 14120–5. doi:10.1016/S0021-9258(17)43831-2. PMID 6196359.
^ abBerg JM (April 1990). "Zinc fingers and other metal-binding domains. Elements for interactions between macromolecules". The Journal of Biological Chemistry. 265 (12): 6513–6. doi:10.1016/S0021-9258(19)39172-0. PMID 2108957.
^Bruno M, Mahgoub M, Macfarlan TS (December 2019). "The Arms Race Between KRAB-Zinc Finger Proteins and Endogenous Retroelements and Its Impact on Mammals". Annual Review of Genetics. 53 (1). Annual Reviews: 393–416. doi:10.1146/annurev-genet-112618-043717. PMID 31518518. S2CID 202572327.
^Cite error: The named reference pmid20192761 was invoked but never defined (see the help page).
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