|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0040624,
umls-concept:C0080055,
umls-concept:C0678594,
umls-concept:C1145667,
umls-concept:C1167622,
umls-concept:C1436059,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2349209,
umls-concept:C2825311
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|
pubmed:issue |
15
|
|
pubmed:dateCreated |
2008-8-8
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|
pubmed:abstractText |
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.
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|
pubmed:language |
eng
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|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
1551-4005
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
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pubmed:volume |
7
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
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pubmed:pagination |
2441-3
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pubmed:meshHeading |
pubmed-meshheading:18677113-Humans,
pubmed-meshheading:18677113-Models, Molecular,
pubmed-meshheading:18677113-Mutant Proteins,
pubmed-meshheading:18677113-Nuclear Proteins,
pubmed-meshheading:18677113-Protein Binding,
pubmed-meshheading:18677113-Protein Conformation,
pubmed-meshheading:18677113-Protein Structure, Tertiary,
pubmed-meshheading:18677113-Proto-Oncogene Proteins,
pubmed-meshheading:18677113-Transcriptional Activation,
pubmed-meshheading:18677113-Tumor Suppressor Protein p53
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|
pubmed:year |
2008
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|
pubmed:articleTitle |
Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain.
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|
pubmed:publicationType |
Letter
|
