1JSP

NMR Structure of CBP Bromodomain in complex with p53 peptide

Summary for 1JSP

• Entry DOI: 10.2210/pdb1jsp/pdb
• Descriptor: tumor protein p53, CREB-BINDING PROTEIN (2 entities in total)
• Functional Keywords: bromodomain, cbp, nmr structure., dna binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637; Cytoplasm: Q92793
• Total number of polymer chains: 2
• Total formula weight: 16825.44

Authors

He, Y.,Mujtaba, S.,Zeng, L.,Yan, S.,Zhou, M.-M. (deposition date: 2001-08-17, release date: 2002-08-17, Last modification date: 2024-10-16)

Primary citation

Mujtaba, S.,He, Y.,Zeng, L.,Yan, S.,Plotnikova, O.,Sachchidanand,Sanchez, R.,Zeleznik-Le, N.J.,Ronai, Z.,Zhou, M.M.
Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation.
Mol.Cell, 13:251-263, 2004

PubMed Abstract: 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. 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. This bromodomain/acetyl-lysine binding is responsible for p53 acetylation-dependent coactivator recruitment after DNA damage, a step essential for p53-induced transcriptional activation of the cyclin-dependent kinase inhibitor p21 in G1 cell cycle arrest. We further present the three-dimensional nuclear magnetic resonance structure of the CBP bromodomain in complex with a lysine 382-acetylated p53 peptide. Using structural and biochemical analyses, we define the molecular determinants for the specificity of this molecular recognition.

PubMed: 14759370
DOI: 10.1016/S1097-2765(03)00528-8

Experimental method

SOLUTION NMR