Helix-turn-helix, zinc-finger, and leucine-zipper motifs for eukaryotic transcriptional regulatory proteins

doi:10.1016/0968-0004(89)90145-X

Trends in Biochemical Sciences

Volume 14, Issue 4, April 1989, Pages 137-140

https://doi.org/10.1016/0968-0004(89)90145-X Get rights and content

Abstract

Four distinct structural motifs have been proposed for the DNA-binding domains of eukaryotic transcriptional regulatory proteins; the helix-turn-helix, two kinds of zinc finger, and the leucine zipper. Within each structural motif, there are often families of related proteins that racognize similar DNA sequences and are conserved throughout the eukaryotic kingdom. However, the processes of transcriptional activation and repression appear to be independent of the specific type of protein-DNA interaction.

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Trends in Biochemical Sciences

ReviewHelix-turn-helix, zinc-finger, and leucine-zipper motifs for eukaryotic transcriptional regulatory proteins

Abstract

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Review
Helix-turn-helix, zinc-finger, and leucine-zipper motifs for eukaryotic transcriptional regulatory proteins