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.
MeSH terms
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Cell Cycle Proteins
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Humans
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Models, Molecular
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Mutant Proteins / chemistry
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Mutant Proteins / metabolism
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Nuclear Proteins / chemistry*
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Nuclear Proteins / metabolism*
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Protein Binding
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Protein Conformation
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Protein Structure, Tertiary / physiology
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Proto-Oncogene Proteins / chemistry*
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Proto-Oncogene Proteins / metabolism*
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Transcriptional Activation / physiology
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Tumor Suppressor Protein p53 / chemistry
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Tumor Suppressor Protein p53 / metabolism*
Substances
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Cell Cycle Proteins
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MDM4 protein, human
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Mutant Proteins
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Nuclear Proteins
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Proto-Oncogene Proteins
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Tumor Suppressor Protein p53