Interactions of coiled coils in transcription factors: where is the specificity?
Amphipathic alpha-helices create the dimerization interface in the bZIP and bHLH classes of DNA-binding proteins. These amphipathic helices have been shown to enter into a wide variety of specific dimerization interactions, and this large array of possible combinatorial interactions may provide for fine control of biological function. In bHLH-ZIP proteins, the addition of a leucine-zipper region immediately carboxyl-terminal to the helix-loop-helix region provides for an additional level of both dimerization specificity and control, again through the interaction of amphipathic alpha-helices. Interhelical electrostatic interactions have been implicated in regulating dimerization specificity.
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National Center for Biotechnology Information, National Institutes of Health, Bethesda, MD 20894.
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D000595:Amino Acid Sequence; D050976:Basic-Leucine Zipper Transcription Factors; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D016384:Consensus Sequence; D004268:DNA-Binding Proteins / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry; D051790:G-Box Binding Factors; D016350:Leucine Zippers; D008958:Models, Molecular; D008969:Molecular Sequence Data; D005810:Multigene Family; D010940:Plant Proteins / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry; D017433:Protein Structure, Secondary; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D014157:Transcription Factors / Q000737:chemistry*
D050976:Basic-Leucine Zipper Transcription Factors; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D051790:G-Box Binding Factors; D010940:Plant Proteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D011494:Protein Kinases