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Mutational analysis of Mdm2 C-terminal tail suggests an evolutionarily conserved role of its length in Mdm2 activity toward p53 and indicates structural differences between Mdm2 homodimers and Mdm2/MdmX heterodimers
Mdm2 can mediate p53 ubiquitylation and degradation either in the form of the Mdm2 homodimer or Mdm2/MdmX heterodimer. The ubiquitin ligase activity of these complexes resides mainly in their respective RING finger domains and also requires adjacent C-terminal tails. So far, structural studies have...
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| Główni autorzy: | , , , |
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| Format: | Artigo |
| Język: | Inglês |
| Wydane: |
Landes Bioscience
2012
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| Hasła przedmiotowe: | |
| Dostęp online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3323797/ https://ncbi.nlm.nih.gov/pubmed/22333590 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.4161/cc.11.5.19445 |
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