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Publication Abstract from PubMed

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.

Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A.,Pavletich NP, Pabo CO Science. 1991 May 10;252(5007):809-17. PMID:2028256^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.