The retroviral oncogene v-myb, and its cellular counterpart c-myb, encode nuclear DNA-binding proteins. In myb, one of the most conserved regions consisting of three tandem repeats has been shown to be involved in DNA-binding [1].

The SANT domain is present in nuclear receptor co-repressors and in the subunits of many chromatin-remodelling complexes [2]. It has a strong structural similarity to the DNA-binding domain of Myb-related proteins [3]. Both consist of tandem repeats of three alpha-helices that are arranged in a helix-turn-helix motif, each alpha helix containing a bulky aromatic residue. Despite the overall similarity there is differences that indicate that the SANT domain is functionally divergent from the canonical Myb DNA-binding domain [4].

1. The highly conserved amino-terminal region of the protein encoded by the v-myb oncogene functions as a DNA-binding domain. EMBO J. 6, 2719-25
2. The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB. Trends Biochem. Sci. 21, 87-8
3. Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI. Mol. Cell 12, 449-60
4. The SANT domain: a unique histone-tail-binding module? Nat. Rev. Mol. Cell Biol. 5, 158-63

The retroviral oncogene v-myb, and its cellular counterpart c-myb, encode nuclear DNA-binding pro
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