Protein zinc finger

CCCH class of zinc finger proteins zinc finger-mediated impairment of cell growth. Gene, 1996, 174(2), 225-33. 

One such regulatory protein, a zinc-finger protein (zinc ion is blue, protein is red), is shown bound to a control region of DNA (black). [(Left) Barnaby Hall/Photonica. (Right) Drawn from lAAY.pdb.]... 

The optimal sequence obtained, called FSD-1 for full sequence design, is shown in Table 17.2 and compared with the sequence of the template Zif 268. A search of the FSD-1 sequence against protein databases did not reveal a statistically significant similarity with any other protein, including zinc finger proteins. 

Examples (a) nucleosome K Huger, AW Mader, RK Richmond, DF Sargent, TJ Richmond. Nature 389 251-260, 1997 (b) DNA polymerases CA Brautigam, TA Steitz. Curr. Opin. Struct. Biol. 8 54-63, 1998 (c) single-stranded binding protein Y Shamoo, AM Friedman, MR Parsons, WH Konigsberg, TA Steitz. Nature 376 362-366, 1995 (d) restriction endonucleases RA Kovall, BW Matthews. Curr. Opin. Chem. Biol. 3 578-583, 1999 (e) DNA lig-ase S Shuman. Structure 4 653-656, 1996 (f) DNA helicases MC Hall, SW Matson. Mol. Microbiol. 34 867-877, 1999 (g) zinc-finger proteins Y Choo, JW Schwabe. Nat. Struct. Biol. 5 253-255, 1998. 

Figure 39-14. Zinc fingers are a series of repeated domains (two to nine) in which each is centered on a tetrahedral coordination with zinc. In the case of TFIIIA, the coordination is provided by a pair of cysteine residues (C) separated by 12-13 amino acids from a pair of histidine (H) residues. In other zinc finger proteins, the second pair also consists of C residues. Zinc fingers bind in the major groove, with adjacent fingers making contact with 5 bp along the same face of the helix.

Zinc-finger protein. A DNA-binding protein that contains a zinc atom. 

There is significant interest in zinc sulfide, selenide, and oxide materials and while extensive discussion is not appropriate here, a number of novel complexes that have been developed for their deposition characteristics of these important semiconductors will be highlighted in the context of the ligand types. Zinc has also been used in supramolecular building blocks as a structural element, much as in zinc finger proteins. In these cases the lack of redox chemistry is... 

Varying ratios of the ligands 7V-(2-thiophenyl)-2,5-dimethylpyrrole and V-methylimidazole were used to form tetrahedral zinc complexes with S4, S3N, and S2N2 coordination spheres. X-ray structural analyses and IR spectra were recorded for all compounds and the relevance to zinc finger proteins was discussed. The comparison to cobalt and cadmium structures showed only minor differences, supporting the theory that changes on substituting these metals into zinc proteins would be minor.538... 

Zinc is a constituent of over 300 enzymes with much research into the coordination of zinc to the protein backbone, and how its chemistry is modulated by the donor set and environment.2 As well as the Lewis acid catalysis properties in enzymes, the structural role in zinc finger proteins has been a major area of research since the late 1990s. A number of reviews on zinc physiology, enzymology, and proteins in general have been published.978-981 There is extensive analysis available to classify the mononuclear sites in zinc proteins and identification of structural relationships of the extended environment.982,983... 

Naested, H., A. Holm et al. (2004). Arabidopsis VARIEGATED 3 encodes a chloroplast-targeted, zinc-finger protein required for chloroplast and palisade cell development. J. Cell. Sci. 117(Pt 20) 4807 1818. 

Beligere, G.S., and Dawson, P.E. (1999) Synthesis of a three zinc finger protein, Zif268, by native chemical ligation. Biopolymers 51(5), 363-369. 

Further research has led to a classification of zinc-finger proteins to include various criteria (1) one or multiple repeat units of about 30 amino acids per finger ... 

---