DAXX protein, also known as a "death-associated factor", is an important player in many cell cycle processes. However the detailed molecular structure of this important protein has not been reported. In this cover article in Structure Lawrence McIntosh (UBC) and his team has discovered using NMR spectroscopy that the C-terminal half of DAXX is intrinsically disordered, whereas the N-terminal portion contains a well-folded helical bundle domain. This important work provides a structural foundation for understanding the diverse functions of DAXX.
E. Escobar-Cabrera, D.K.W. Lau, S. Giovinazzi, A.M. Ishov, L.P. McIntosh, "Structural Characterization of the DAXX N-Terminal Helical Bundle Domain and Its Complex with Rassf1C," Structure 18 (2010) 1642–1653. (Cover Article) http://dx.doi.org/10.1016/j.str.2010.09.016