A homodimerization protein interaction domain occurring at the N terminus of proteins that contain multiple copies of either CYS2-HIS2 ZINC FINGERS or KELCH REPEATS. It is characterized by a tightly intertwined dimer with an extensive hydrophobic interface. A surface-exposed groove lined with conserved amino acids is formed at the dimer interface, suggesting a peptide-binding site. Many BTB proteins are transcriptional regulators that are thought to regulate CHROMATIN structure.
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