The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition

@article{Fairall1993TheCS,
  title={The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition},
  author={Louise Fairall and John W. R. Schwabe and Lynda Chapman and John T. Finch and Daniela Rhodes},
  journal={Nature},
  year={1993},
  volume={366},
  pages={483-487}
}
THE Cys2-His2 zinc-finger is the most widely occurring DNA-binding motif1–3. The first structure of a zinc-finger/DNA complex revealed a fairly simple mechanism for DNA recognition4 suggesting that the zinc-finger might represent a candidate template for designing proteins to recognize DNA5. Residues at three key positions in an α-helical 'reading head' play a dominant role in base-recognition and have been targets for mutagenesis experiments aimed at deriving a recognition code6–8. Here we… 

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TLDR
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Zinc fingers
  • A. Klug, J. Schwabe
  • Chemistry, Medicine
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1995
The term zinc finger was first used to describe a 30‐residue, repeated sequence motif found in an unusually abundant Xenopus transcription factor. It was proposed that each motif is folded around a
DNA-induced α-helix capping in conserved linker sequences is a determinant of binding affinity in Cys2-His2 zinc fingers
Abstract High-affinity, sequence-specific DNA binding by Cys2-His2 zinc finger proteins is mediated by both specific protein-base interactions and non-specific contacts between charged side-chains
New Insights into DNA Recognition by Zinc Fingers Revealed by Structural Analysis of the Oncoprotein ZNF217*
TLDR
The structure of a ZNF217-DNA complex is determined and it is shown that although the overall position of the ZFs on the DNA closely resembles that observed for other ZFs, the side-chain interaction pattern differs substantially from the canonical model.
The Multi-zinc Finger Protein ZNF217 Contacts DNA through a Two-finger Domain*
Background: Classical C2H2 zinc finger proteins generally bind DNA via a three-finger motif. Results: We have identified the DNA site recognized by ZNF217 and defined its mechanism of binding.
GAGA: Structural Basis for Single Cys2His2 Zinc Finger-DNA Interaction
The structural basis of sequence specific binding of the Cys2His2 single zinc finger DNA binding domain of the transcription factor GAGA is explored on the basis of the three-dimensional structure of
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