3dab | pdb_00003dab
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Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain
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Structural highlights
FunctionMDM4_HUMAN Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions.[1] [2] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain.,Popowicz GM, Czarna A, Holak TA Cell Cycle. 2008 Aug;7(15):2441-3. Epub 2008 May 27. PMID:18677113[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 15:06, 1 November 2023.