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

FEBS Letters

Briggs, Judith A.¹  Briggs, Robert C.¹  Xie, Jingping¹ 

[1] Department of Pathology, Vanderbilt University Medical School, Nashville TN 37232-5310, USA

关键词: MNDA;    Cross-linking;    Dimerization;    Mutation;   

DOI  :  10.1016/S0014-5793(97)00404-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown