Myc transcription factors have a bHLHZip domain and are associated with transcriptional activation of genes involved in cell growth and apoptosis. In order to activate those genes, Myc forms a heterodimer with Max via a leucin zipper which enables the dimer to bind to DNA. Max is a structurally related transcription factor that can also form homodimers. Omo-Myc is a non-native miniprotein derived from the bHLHZip domain of Myc. It carries four mutations which enable it not only to homodimerize efficiently but also to form heterodimers with Myc and Max. As Myc cannot form homodimers, this model will take you through these different mutations and explain their relevance for dimer formation.
References: Soucek et al (1998) Oncogene 17 2463-2472 Soucek et al (2002) Cancer Research 62 3507-3510 Carl Brandon and John Tooze (1999) Introduction to Protein Structure 2 201
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