Abstract
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 partway 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 α helix contact the bases, and most of the contacts 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.
Keywords
Zinc fingerDNAProtein–DNA interactionLIM domainDNA binding siteHMG-boxGuanineCrystallographyBiologyBase pairDNA-binding proteinBinding siteChemistryGeneBiophysicsBiochemistryGene expressionTranscription factorNucleotidePromoter
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Publication Info
- Year
- 1991
- Type
- article
- Volume
- 252
- Issue
- 5007
- Pages
- 809-817
- Citations
- 2062
- Access
- Closed
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Cite This
Nikola P. Pavletich,
Carl O. Pabo
(1991).
Zinc Finger-DNA Recognition: Crystal Structure of a Zif268-DNA Complex at 2.1 Å.
Science
, 252
(5007)
, 809-817.
https://doi.org/10.1126/science.2028256
Identifiers
- DOI
- 10.1126/science.2028256