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MNDA dimerizes through a complex motif involving an N‐terminal basic region
Author(s) -
Xie Jingping,
Briggs Judith A.,
Briggs Robert C.
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00404-3
Subject(s) - biology , computational biology , leucine zipper , genetics , gene , transcription factor
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.