Abstract
The helix-loop-helix proteins are characterized by a highly conserved 60-100 residue motif comprised of two amphipathic α-helices separated by a loop of variable length, and amino acid composition and sequence. These motifs dimerize by approximating the conserved hydrophobic faces of the α-helices, forming a left-handed, parallel, four-helix bundle. Baltimore and coworkers (Murre et al. 1989) first described conservation of this feature in a large number of eukaryotic transcription factors, and implicated it in dimerization and DNA binding. Subsequent work has confirmed their bold prediction and demonstrated that the helix-loop-helix motif is primarily responsible for dimerization. Most helix-loop-helix proteins possess a highly conserved basic region immediately N-terminal to the first helix (Prendergast and Ziff 1989), which mediates high-affinity, specific DNA binding (reviewed in Bexevanis and Vinson 1993). In addition, the second helix of many of these transcription factors is extended beyond the C-terminus of the fourhelix bundle, where a leucine heptad repeat or zipper forms a left-handed, coiled-coil dimer interface. Finally, some helix-loop-helix proteins lack the basic region (Benezra et al. 1990).
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© 1995 Springer-Verlag Berlin Heidelberg
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Ferré-D’Amaré, A.R., Burley, S.K. (1995). DNA Recognition by Helix-Loop-Helix Proteins. In: Eckstein, F., Lilley, D.M.J. (eds) Nucleic Acids and Molecular Biology. Nucleic Acids and Molecular Biology, vol 9. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79488-9_14
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DOI: https://doi.org/10.1007/978-3-642-79488-9_14
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