Dimers, leucine zippers and DNA-binding domains

Trends Genet. 1990 Feb;6(2):36-40. doi: 10.1016/0168-9525(90)90071-d.

Abstract

Transcription factors can be divided into classes on the basis of their mode of interaction with the target promoter sequence. Different protein domains responsible for DNA recognition have been identified. In this review we discuss the leucine zipper structure, which has been found in several nuclear factors, including the oncoproteins Fos and Jun. Structural considerations are summarized to help understand how dimerization is mediated by the leucine zipper and how this is the prerequisite for optimal target DNA recognition by the adjacent basic domains.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • DNA / metabolism*
  • Gene Expression Regulation
  • Leucine*
  • Molecular Sequence Data
  • Sequence Homology, Nucleic Acid
  • Transcription Factors / genetics*

Substances

  • Transcription Factors
  • DNA
  • Leucine