Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comparative Study
. 1991 Feb 1;88(3):999-1003.
doi: 10.1073/pnas.88.3.999.

Zinc fingers, zinc clusters, and zinc twists in DNA-binding protein domains

B L Vallee  1 , J E Coleman, D S Auld
Affiliations
Comparative Study

Zinc fingers, zinc clusters, and zinc twists in DNA-binding protein domains

B L Vallee et al. Proc Natl Acad Sci U S A. .

Abstract

We now recognize three distinct motifs of DNA-binding zinc proteins: (i) zinc fingers, (ii) zinc clusters, and (iii) zinc twists. Until very recently, x-ray crystallographic or NMR three-dimensional structure analyses of DNA-binding zinc proteins have not been available to serve as standards of reference for the zinc binding sites of these families of proteins. Those of the DNA-binding domains of the fungal transcription factor GAL4 and the rat glucocorticoid receptor are the first to have been determined. Both proteins contain two zinc binding sites, and in both, cysteine residues are the sole zinc ligands. In GAL4, two zinc atoms are bound to six cysteine residues which form a "zinc cluster" akin to that of metallothionein; the distance between the two zinc atoms of GAL4 is approximately 3.5 A. In the glucocorticoid receptor, each zinc atom is bound to four cysteine residues; the interatomic zinc-zinc distance is approximately 13 A, and in this instance, a "zinc twist" is represented by a helical DNA recognition site located between the two zinc atoms. Zinc clusters and zinc twists are here recognized as two distinctive motifs in DNA-binding proteins containing multiple zinc atoms. For native "zinc fingers," structural data do not exist as yet; consequently, the interatomic distances between zinc atoms are not known. As further structural data become available, the structural and functional significance of these different motifs in their binding to DNA and other proteins participating in the transmission of the genetic message will become apparent.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. J Mol Biol. 1984 Dec 5;180(2):239-50 - PubMed
    1. Proc Natl Acad Sci U S A. 1989 Jan;86(1):327-31 - PubMed
    1. Nature. 1987 Jul 23-29;328(6128):353-5 - PubMed
    1. Biochem Biophys Res Commun. 1987 Mar 13;143(2):740-8 - PubMed
    1. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9045-9 - PubMed

Publication types