@article { ISI:000285221100012,
	title = {Structural Characterization of the DAXX N-Terminal Helical Bundle Domain and Its Complex with Rassf1C},
	journal = {STRUCTURE},
	volume = {18},
	number = {12},
	year = {2010},
	month = {DEC 8},
	pages = {1642-1653},
	abstract = {DAXX is a scaffold protein with diverse roles including transcription and cell cycle regulation. Using NMR spectroscopy, we demonstrate that the C-terminal half of DAXX is intrinsically disordered, whereas a folded domain is present near its N terminus. This domain forms a left-handed four-helix bundle (H1, H2, H4, H5). However, due to a crossover helix (H3), this topology differs from that of the Sin3 PAH domain, which to date has been used as a model for DAXX. The N-terminal residues of the tumor suppressor Rassf1C fold into an amphipathic alpha helix upon binding this DAXX domain via a shallow cleft along the flexible helices H2 and H5 (K(D) similar to 60 mu M). Based on a proposed DAXX recognition motif as hydrophobic residues preceded by negatively charged groups, we found that peptide models of p53 and Mdm2 also bound the helical bundle. These data provide a structural foundation for understanding the diverse functions of DAXX.},
	issn = {0969-2126},
	doi = {10.1016/j.str.2010.09.016},
	author = {Escobar-Cabrera, Eric and Lau, Desmond K. W. and Giovinazzi, Serena and Ishov, Alexander M. and McIntosh, Lawrence P.}
}
