Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A

@article{Pavletich1991ZincFR,
  title={Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A},
  author={N. P. Pavletich and C. O. Pabo},
  journal={Science},
  year={1991},
  volume={252},
  pages={809 - 817}
}
The zinc finger DNA-binding motif occurs in many proteins that regulate eukaryotic gene expression. The crystal structure of a complex containing the three zinc fingers from Zif268 (a mouse immediate early protein) and a consensus DNA-binding site has been determined at 2.1 angstroms resolution and refined to a crystallographic R factor of 18.2 percent. In this complex, the zinc fingers bind in the major groove of B-DNA and wrap part way around the double helix. Each finger has a similar… 

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The crystal structure of a complex containing the five Zn fingers from the human GLI oncogene and a high-affinity DNA binding site has been determined and Analyzing the GLI complex and comparing it with Zif268 offers new perspectives on Zn finger-DNA recognition.

Solution structure of the first three zinc fingers of TFIIIA bound to the cognate DNA sequence: determinants of affinity and sequence specificity.

The high resolution solution structure of a protein containing the three amino-terminal zinc fingers of Xenopus laevis transcription factor IIIA bound to its cognate DNA duplex was determined by nuclear magnetic resonance spectroscopy and provides a molecular level explanation for the large body of footprinting and mutagenesis data available for the TFIIIA-DNA complex.

An arginine residue instead of a conserved leucine residue in the recognition helix of the finger 3 of Zif268 stabilizes the domain structure and mediates DNA binding.

Results demonstrate that, as with the Leu residue, the aliphatic carbon side chain of this Arg residue plays a key role in the formation of a stable zinc finger domain, and its terminal guanidinium group appears to be essential for DNA binding mediated through both electrostatic interaction and hydrogen bonding with DNA phosphate backbone.

Invariance of the zinc finger module: A comparison of the free structure with those in nucleic‐acid complexes

The general conclusion is that RNA is recognized by zinc fingers through a combination of its different kinds of structural elements.

New Insights into DNA Recognition by Zinc Fingers Revealed by Structural Analysis of the Oncoprotein ZNF217*

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.
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