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

FEBS Letters
J XieR C Briggs

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 alpha-helical region which was not required for dimerization.

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Citations

Sep 23, 2003·Journal of Molecular Biology·Edvards LiepinshGottfried Otting
May 18, 2005·Experimental Cell Research·Louise E A LudlowChristopher J P Clarke
Dec 29, 1998·Biochimie·S LandolfoD Lembo
Feb 13, 2001·Trends in Biochemical Sciences·E StaubA Rosenthal
Feb 13, 2001·Trends in Biochemical Sciences·K PawłowskiA Godzik
Jan 24, 2004·Journal of Experimental Botany·Sébastien BaudChristine Rochat
Apr 17, 2010·American Journal of Respiratory and Critical Care Medicine·Nasser Fotouhi-ArdakaniEric Milot
Sep 10, 2014·Biochemical Pharmacology·Dympna J Connolly, Andrew G Bowie
Dec 8, 2004·Biochemical and Biophysical Research Communications·Kim S CresswellRicky W Johnstone
Sep 6, 2007·Journal of Cellular Biochemistry·Louise E LudlowRicky W Johnstone
Mar 22, 2005·Journal of Cellular Biochemistry·Robert C BriggsRoberto N Miranda
Aug 24, 1999·Molecular and Cellular Biology·R W Johnstone, J A Trapani

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