Zinc finger motif binding

Sukegawa, J., and Blobel, G. (1993). A nuclear pore complex protein that contains zinc finger motifs, binds DNA and faces the nucleoplasm. Cell (Cambridge, Mass.) 72, 29-38. 

Proteins with the helix-turn-helix or leucine zipper motifs form symmetric dimers, and their respective DNA binding sites are symmetric palindromes. In proteins with the zinc finger motif, the binding site is repeated two to nine times. These features allow for cooperative interactions between binding sites and enhance the degree and affinity of binding. 

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.)...

Figure 2. Structural and functional domains of PARP-1. PARP-1 has a highly conserved structural and functional organization including (1) an N-terminal DNA binding domain with two Cys-Cys-His-Cys zinc finger motifs (FI and Fll), (2) a nuclear localization signal (NLS), (3) a central automodification domain containing a BRCT ( BRCAl C-terminus-like ) protein-protein interaction motif, and (4) a C-terminal catalytic domain with a contiguous 50 amino acid sequence, the PARP signature motif, that forms the active site...

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