Tandem zinc fingers

Blackshear P J (2002). Tristetraprolin and other CCCH tandem zinc-finger proteins in the regulation of mRNA turnover. Biochem. Soc. Trans. 30 945-952. 

Blackshear P J, Lai W S, Kennington E A, et al. (2003). Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates. J. Biol. Chem. 278 19947-19955. 

The classic zinc fingers bind to DNA in tandem along the major groove... 

Figure 10.3 Schematic diagram of the stmcture of three zinc fingers of Zif 268 bound to DNA. The three zinc fingers, which bind In tandem to the major groove of DNA, are colored blue, red and green from the N-terminus. The zinc fingers have the same stmcture and bind in a similar way with the N-terminus of the a helix pointing into the major groove. (Adapted from N.P. Pavletich et al.. Science 261 1701-1707, 1993.)...

Figure 12.14 (Left) Schematic representation of tandemly repeated zinc finger motif with their tetrahedrally coordinated Zn2+ ions. Conserved amino acids are labelled, and the most probable DNA-binding side chains are indicated by balls (from Klug and Rhodes, 1988). (Right) A ribbon diagram of a single zinc finger motif in a ribbon diagram representation. (From Voet and Voet, 2004. Reproduced with permission from John Wiley Sons., Inc.)...

The co-repressor KAP-1 functionally links the DNA-binding Kruppel-associated box zinc finger proteins to the NURD complex by recruiting the Mi-2a subunit. [251]. This interaction requires a tandem PHD/bromodomain motif in which the individual domains appear to act together as a functional unit. The nature of any possible acetylated lysine targets of the bromodomain remains unclear but it is not excluded that this domain could bind to an acetylated lysine in Mi-2a rather than to an acetylated histone tail. 

Fig. 8. Cys2-His2 zinc finger DNA-binding proteins contain multiple tandem repeats of zinc finger domains. A ribbon representation of a six-zinc-finger protein (white) is wrapped around the major groove of DNA (black). A single domain (right) consists of two /3-strands and an ce-helix. A zinc atom (sphere) is coordinated by two cystines and two histidines. Sequence-specific contacts with the DNA occur at the A-terminus of the ce-helix (top right of domain shown at right).

Each zinc finger forms a compact Pfia structure (see Figure 1(d)) and basic and hydrophobic amino acids on the surface of the ct-helix make specific contacts with the edges of the nucleotide bases in the major groove of the Two or more C2 H2 zinc fingers arranged in tandem are required... 

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