Dimers, leucine zippers and DNA-binding domains.
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.
Laboratoire de Génétique Moléculaire des Eucaryotes du CNRS, Unité 184 de l'Inserm, Institut de Chimie Biologique, Strasbourg, France.
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SJ
Busch
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Sassone-Corsi
D000595:Amino Acid Sequence; D004247:DNA / Q000378:metabolism*; D005786:Gene Expression Regulation; D007930:Leucine; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D014157:Transcription Factors / Q000235:genetics*
D014157:Transcription Factors; D004247:DNA; D007930:Leucine