The Mdmx oncoprotein has only recently emerged as a critical-independent to Mdm2-regulator of p53 activation. We have determined the crystal structure of the N-terminal domain of human Mdmx bound to a 15-residue transactivation domain peptide of human p53. The structure shows why antagonists of the Mdm2 binding to p53 are ineffective in the Mdmx-p53 interaction. ©2008 Landes Bioscience.
CITATION STYLE
Popowicz, G. M., Czarna, A., & Holak, T. A. (2008). Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain. Cell Cycle, 7(15), 2441–2443. https://doi.org/10.4161/cc.6365
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