InterPro domain: IPR036671

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [ 1 , 2 , 3 , 4 , 5 ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [ 6 ]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.

This entry represents the DPH-type metal binding domain consists of a three-stranded beta-sandwich with one sheet comprising two parallel strands: (i) beta1 and (ii) beta6 and one anti-parallel strand: beta5. The second sheet in the beta-sandwich is comprised of strands beta2, beta3, and beta4 running anti-parallel to each other. The two beta-sheets are separated by a short stretch alpha-helix.It can be found in proteins such as DPH3 and DPH4. This domain is also found associated with N-terminal domain of heat shock protein DnaJ IPR001623 domain [ 7 , 8 , 9 ].

1. Zinc finger peptides for the regulation of gene expression. J. Mol. Biol. 293, 215-8
2. Multiple modes of RNA recognition by zinc finger proteins. Curr. Opin. Struct. Biol. 15, 367-73
3. Zinc finger proteins: getting a grip on RNA. Curr. Opin. Struct. Biol. 15, 94-8
4. Sticky fingers: zinc-fingers as protein-recognition motifs. Trends Biochem. Sci. 32, 63-70
5. Zinc fingers--folds for many occasions. IUBMB Life 54, 351-5
6. Zinc finger proteins: new insights into structural and functional diversity. Curr. Opin. Struct. Biol. 11, 39-46
7. Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module. Biochemistry 44, 8801-9
8. Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4. J. Biol. Chem. 287, 13194-205
9. Structure of the Kti11/Kti13 heterodimer and its double role in modifications of tRNA and eukaryotic elongation factor 2. Structure 23, 149-160