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

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Abstract
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 α‐helical region which was not required for dimerization.