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Science 10 May 1991:
Vol. 252. no. 5007, pp. 809 - 817
DOI: 10.1126/science.2028256
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Articles

Science, Vol 252, Issue 5007, 809-817
Copyright © 1991 by American Association for the Advancement of Science

articles

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

NP Pavletich and CO Pabo

Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.

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 relation to the DNA and makes its primary contacts in a three-base pair subsite. Residues from the amino-terminal portion of an alpha helix contact the bases, and most of the contracts are made with the guanine-rich strand of the DNA. This structure provides a framework for understanding how zinc fingers recognize DNA and suggests that this motif may provide a useful basis for the design of novel DNA-binding proteins.


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J. Biol. Chem. 277, 3850-3856
   Abstract »    Full Text »    PDF »
A. thaliana TRANSPARENT TESTA 1 is involved in seed coat development and defines the WIP subfamily of plant zinc finger proteins.
M. Sagasser, G.-H. Lu, K. Hahlbrock, and B. Weisshaar (2002)
Genes & Dev. 16, 138-149
   Abstract »    Full Text »    PDF »
Selected base sequence outside the target binding site of zinc finger protein Sp1.
M. Nagaoka, Y. Shiraishi, and Y. Sugiura (2001)
Nucleic Acids Res. 29, 4920-4929
   Abstract »    Full Text »    PDF »
Role of CACC-Box in the Regulation of Ovine Follicle-Stimulating Hormone Receptor Expression.
W. Xing and M. R. Sairam (2001)
Biol Reprod 65, 1142-1149
   Abstract »    Full Text »    PDF »
Site-Specific Acetylation by p300 or CREB Binding Protein Regulates Erythroid Kruppel-Like Factor Transcriptional Activity via Its Interaction with the SWI-SNF Complex.
W. Zhang, S. Kadam, B. M. Emerson, and J. J. Bieker (2001)
Mol. Cell. Biol. 21, 2413-2422
   Abstract »    Full Text »
Sequence-Specific Transcriptional Repression by KS1, a Multiple-Zinc-Finger-Kruppel-Associated Box Protein.
B. Gebelein and R. Urrutia (2001)
Mol. Cell. Biol. 21, 928-939
   Abstract »    Full Text »
A novel four zinc-finger protein targeted against p190BcrAbl fusion oncogene cDNA: utilisation of zinc-finger recognition codes.
A. R. McNamara and K. G. Ford (2000)
Nucleic Acids Res. 28, 4865-4872
   Abstract »    Full Text »    PDF »


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