3dac
Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domainStructure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain
Structural highlights
FunctionMDM4_DANRE Inhibits p53- and p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain (By similarity). Evolutionary ConservationCheck, 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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