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Curr Opin Genet Dev. 1993 Apr;3(2):278-85.

Interactions of coiled coils in transcription factors: where is the specificity?

Author information

1
National Center for Biotechnology Information, National Institutes of Health, Bethesda, MD 20894.

Abstract

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.

PMID:
8504253
DOI:
10.1016/0959-437x(93)90035-n
[Indexed for MEDLINE]

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