Zinc Fingers‐‐Folds for Many Occasions

  title={Zinc Fingers‐‐Folds for Many Occasions},
  author={Jacqueline M Matthews and Margaret Sunde},
  journal={IUBMB Life},
Zinc finger domains (ZnFs) are common, relatively small protein motifs that fold around one or more zinc ions. In addition to their role as a DNA‐binding module, ZnFs have recently been shown to mediate protein:protein and protein:lipid interactions. This small zinc‐ligating domain, often found in clusters containing fingers with different binding specificities, can facilitate multiple, often independent intermolecular interactions between nucleic acids and proteins. Classical ZnFs, typified by… 
Structural Analyses of Zinc Finger Domains for Specific Interactions with DNA.
The structural information in this study will aid in the selection of unique types of zinc finger applications in vivo and in vitro approaches, because biophysical backgrounds including complex structures and binding affinities aid inThe protein design area.
Neural Zinc Finger Factor/Myelin Transcription Factor Proteins: Metal Binding, Fold, and Function.
One class of nonclassical ZFs, the neural zinc finger/myelin transcription factor (NZF/MyT) class, contains ZF domains with a Cys2His2Cys ligand set, adopts a fold that consists of a series of loops in the presence of zinc, and functions as transcription factors by binding to and regulating genes that are critical for the development of the central nervous system.
Zinc: DNA‐Binding Proteins
Zinc-containing nucleic acid-binding proteins are ubiquitous in nature and interact with all types of nucleic acids, including ssDNA, duplex DNA, and RNA. The primary role played by these Zn(II)
Structural metal sites in nonclassical zinc finger proteins involved in transcriptional and translational regulation.
This Account focuses on the laboratory's efforts to characterize two families of "nonclassical" ZFs: the Cys3His (or CCCH) ZF family and the CYS2His2Cys (or CCHHC) ZFs family, a small family of nonclassical ZFs that are essential for the development of the central nervous system.
Keep Your Fingers Off My DNA: Protein–Protein Interactions Mediated by C2H2 Zinc Finger Domains
The current knowledge of over 100 C2H2 zinc finger-mediated PPIs is reviewed, focusing on what is known about the binding surface, contributions of individual fingers to the interaction, and function.
Zinc binding of Tim10: Evidence for existence of an unstructured binding intermediate for a zinc finger protein
A two‐step reaction model mechanism is proposed, in which zinc‐binding is regulated by the initial selective‐binding of Zn2+ to Cys followed by folding, which is consistent with that of the studies at equilibrium.
Metal binding properties, stability and reactivity of zinc fingers
Abstract Zinc fingers (ZFs) are among the most structurally diverse protein domains. They interact with nucleic acids, other proteins and lipids to facilitate a multitude of biological processes.
Cysteine and histidine shuffling: mixing and matching cysteine and histidine residues in zinc finger proteins to afford different folds and function.
These proteins bind zinc in a tetrahedral geometry, like the classical zinc finger proteins, yet they adopt completely different folds and target different oligonucleotides, suggesting that the relationships between metal coordination and protein structure/function are less defined.
Protein-protein interactions mediated by Cys2His2 zinc-fingers
Analysis of the interaction specificities of the Ikaros and Hunchback transcription factor domains led to the discovery of a novel anti-parallel interaction mode for the DZF domain, suggesting that the importance of the D ZF domain is due to its ability to mediate dimerization.
The Protein-Binding Potential of C2H2 Zinc Finger Domains
The primary conclusion is that DNA binding is a more restricted function of ZFs, and that their potential for mediating protein interactions is likely greater, suggesting that the role of C2H2 ZF domains in protein interactions has probably been underestimated.