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

  title={Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A},
  author={N. P. Pavletich and C. O. Pabo},
  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… 

Crystal structure of a five-finger GLI-DNA complex: new perspectives on zinc fingers.

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.

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.

Zinc fingers

  • A. KlugJ. Schwabe
  • Biology
    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

A zinc finger directory for high-affinity DNA recognition.

  • A. JamiesonH. WangS. Kim
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1996
We have used two monovalent phage display libraries containing variants of the Zif268 DNA-binding domain to obtain families of zinc fingers that bind to alterations in the last 4 bp of the DNA

DNA-induced α-helix capping in conserved linker sequences is a determinant of binding affinity in Cys2-His2 zinc fingers

NMR evidence is presented for another contribution to high-affinity binding, a highly specific DNA-induced helix capping involving residues in the linker sequence between fingers, which is suggested to provide a rationale for the high conservation of the TGEKP linker sequences in Cys2-His2 zinc finger proteins.



Base sequence discrimination by zinc-finger DNA-binding domains

The results show that each finger spans three nucleotides and indicate two positions in Krox-20 zinc fingers that are important for base-pair selectivity, and modelling with molecular graphics suggests that these residues could bind directly with the bases and that other amino acid–base contacts are also possible.

Zinc-dependent structure of a single-finger domain of yeast ADR1.

An experimentally determined model of thesingle finger is proposed that is consistent with circular dichroism, one- and two-dimensional nuclear magnetic resonance, and visual spectroscopy of the single-finger peptide reconstituted in the presence of zinc.

Three-dimensional solution structure of a single zinc finger DNA-binding domain.

The three-dimensional solution structure of a zinc finger nucleic acid binding motif has been determined by nuclear magnetic resonance (NMR) spectroscopy. Spectra of a synthetic peptide corresponding

Proposed structure for the zinc-binding domains from transcription factor IIIA and related proteins.

  • J. Berg
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1988
The proposed structure provides a basis for understanding the detailed roles of the conserved residues and allows construction of a model for the interaction of these proteins with nucleic acid in which the proteins wrap around the nucleic acids in the major groove.

Repetitive zinc‐binding domains in the protein transcription factor IIIA from Xenopus oocytes.

Analysis of the amino acid sequence reveals nine tandem similar units, each consisting of approximately 30 residues and containing two invariant pairs of cysteines and histidines, the most common ligands for zinc in the 7S particle of Xenopus laevis oocytes, which suggests that the protein contains repetitive zinc‐binding domains.

Structure of the lambda complex at 2.5 A resolution: details of the repressor-operator interactions

The crystal structure of a complex containing the DNA-binding domain of lambda repressor and a lambda operator site was determined at 2.5 A resolution and refined to a crystallographic R factor of

Solution structure of the glucocorticoid receptor DNA-binding domain.

A model of the dimeric complex between the DBD and the glucocorticoid response element is proposed, consistent with previous results indicating that specific amino acid residues of the D BD are involved in protein-DNA and protein-protein interactions.

DNA binding site of the growth factor-inducible protein Zif268.

  • B. ChristyD. Nathans
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1989
Zif268 synthesized in Escherichia coli bound to two sites upstream of the zif268 gene and to sites in the promoter regions of other genes, resulting in the following consensus sequence for a Zif268 high-affinity binding site: GCGTGGGGCG.