Abstract
Recently determined structures of a number of Myc family proteins have provided significant insights into themolecular nature of complex assembly and DNA binding. These structures illuminate the details of specific interactions that govern the assembly of nucleoprotein complexes and, in doing so, raisemore questions regarding Myc biology. In this review, we focus on the lessons provided by these structures toward understanding (1) interactions that govern transcriptional repression by Mad via the Sin3 pathway, (2) homodimerization of Max, (3) heterodimerization of Myc-Max and Mad-Max, and (4) DNA recognition by each of the Max-Max, Myc-Max, and Mad-Max dimers.
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Keywords
- Leucine Zipper
- Leucine Zipper Region
- Amino Terminal Residue
- Harb Symp Quant Biol
- Spring Harb Symp Quant Biol
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Nair, S.K., Burley, S.K. (2006). Structural Aspects of Interactions Within the Myc/Max/Mad Network. In: Eisenman, R.N. (eds) The Myc/Max/Mad Transcription Factor Network. Current Topics in Microbiology and Immunology, vol 302. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-32952-8_5
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DOI: https://doi.org/10.1007/3-540-32952-8_5
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