Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain
Year: 2008
Type: article
Abstract: 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.
Source: Cell Cycle
DOI: 10.4161/cc.6365
Authors: Grzegorz Popowicz, Anna Czarna, Tad Holak
Institutions: Max Planck Society, Max Planck Institute of Biochemistry
Language: English
Subfield: Oncology
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
OpenAlex ID: W2116416768