3LW1

Binary complex of 14-3-3 sigma and p53 pT387-peptide

Summary for 3LW1

• Entry DOI: 10.2210/pdb3lw1/pdb
• Related: 1ywt 1yz5 2o02 2o98 3cu8 3e6y
• Descriptor: 14-3-3 protein sigma, peptide of Cellular tumor antigen p53, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: adapter protein, cytoplasm, nucleus, phosphoprotein, peptide binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P31947; Cytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637
• Total number of polymer chains: 2
• Total formula weight: 29502.97

Authors

Schumacher, B.,Mondry, J.,Thiel, P.,Weyand, M.,Ottmann, C. (deposition date: 2010-02-23, release date: 2010-03-23, Last modification date: 2023-11-22)

Primary citation

Schumacher, B.,Mondry, J.,Thiel, P.,Weyand, M.,Ottmann, C.
Structure of the p53 C-terminus bound to 14-3-3: Implications for stabilization of the p53 tetramer
Febs Lett., 584:1443-1448, 2010

PubMed Abstract: The adaptor protein 14-3-3 binds to and stabilizes the tumor suppressor p53 and enhances its anti-tumour activity. In the regulatory C-terminal domain of p53 several 14-3-3 binding motifs have been identified. Here, we report the crystal structure of the extreme C-terminus (residues 385-393, p53pT387) of p53 in complex with 14-3-3sigma at a resolution of 1.28A. p53pT387 is accommodated by 14-3-3 in a yet unrecognized fashion implying a rationale for 14-3-3 binding to the active p53 tetramer. The structure exhibits a potential binding site for small molecules that could stabilize the p53/14-3-3 protein complex suggesting the possibility for therapeutic intervention.

PubMed: 20206173
DOI: 10.1016/j.febslet.2010.02.065

Experimental method

X-RAY DIFFRACTION (1.28 Å)