Omo-myc homodimer bound to DNA

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Myc transcription factors boast a bHLHZip domain, and are intricately linked with the activation of genes governing cell growth and apoptosis. To activate these 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 on its own. Omo-Myc is a non-native miniprotein derived from the bHLHZip domain of Myc, carrying four mutations that not only allow it to efficiently form homodimers but also enable it to form heterodimers with both Myc and Max. Since Myc cannot form homodimers on its own, 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