Title : Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation.

Pub. Date : 2004 Jan 30

PMID : 14759370






3 Functional Relationships(s)
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1 Lysine acetylation of the tumor suppressor protein p53 in response to a wide variety of cellular stress signals is required for its activation as a transcription factor that regulates cell cycle arrest, senescence, or apoptosis. Lysine tumor protein p53 Homo sapiens
2 Here, we report that the conserved bromo-domain of the transcriptional coactivator CBP (CREB binding protein) binds specifically to p53 at the C-terminal acetylated lysine 382. Lysine tumor protein p53 Homo sapiens
3 We further present the three-dimensional nuclear magnetic resonance structure of the CBP bromodomain in complex with a lysine 382-acetylated p53 peptide. Lysine tumor protein p53 Homo sapiens