MNDA dimerizes through a complex motif involving an N-terminal basic region.

Human myeloid cell nuclear differentiation antigen (MNDA) is a myelomonocytic lineage-specific protein that influences gene expression through interactions with other nuclear proteins and transcription factors. MNDA also self-associates and chemical cross-linking was used to demonstrate that MNDA forms a dimer. C-terminal and internal deletion mutants were used to identify two regions in the N-terminal half of MNDA essential for self-association. One region contains an imperfect leucine zipper and the second is highly enriched in basic residues. The sequences that are essential for dimerization are separated by a highly basic amphipathic alpha-helical region which was not required for dimerization.