Abstract
Many DNA binding proteins dimerize and interact with palindromic DNA sequences to regulate gene expression (for review see 1). One class of DNA-binding proteins has been shown to dimerize through a leucine zipper structural motif. A domain of basic amino acids, immediately 5’ to the heptad leucine repeat, mediates specific chemical interactions with DNA and is responsible for binding specificity. Protein dimers can not bind DNA unless there are two functional basic domains (2).
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Taylor, N., Kolman, J.L., Miller, G. (1991). Heterodimers of the Zebra and Fos Basic Domains Bind DNA with the Specificity of Zebra. In: Ablashi, D.V., Huang, A.T., Pagano, J.S., Pearson, G.R., Yang, C.S., Ablashi, K.L. (eds) Epstein-Barr Virus and Human Disease · 1990. Experimental Biology and Medicine, vol 24. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-4612-0405-3_15
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DOI: https://doi.org/10.1007/978-1-4612-0405-3_15
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-4612-6747-8
Online ISBN: 978-1-4612-0405-3
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