The MafB:cFos heterodimeric complex comprises two distinct transcription factors, MafB and cFos, intricately assembled to regulate gene expression by binding to DNA. This complex exhibits a distinctive Y-shaped structure, facilitated by the presence of a leucine zipper region at the dimerization interface. Here, hydrophobic interactions among leucine residues promote the binding of the two proteins, resulting in the formation of a stable coiled structure reminiscent of a Y-shape.
MafB, an alkaline leucine zipper (bZIP) transcription factor, plays a pivotal role in regulating lineage-specific hematopoiesis and is implicated in various developmental processes, including tumorigenesis, differentiation, and hematopoiesis (Pogenberg et al., 2014). On the other hand, c-Fos is a key player in cancer development, exerting its influence on vital cellular events such as proliferation, differentiation, and survival (Tulchinsky, 2000) ructure, 22(2), 1-7. DOI: 10.1016/j.str.2013.12.017.
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