期刊
FEBS LETTERS
卷 584, 期 8, 页码 1443-1448出版社
WILEY
DOI: 10.1016/j.febslet.2010.02.065
关键词
14-3-3 protein; Protein-protein interaction; Stabilizing molecule; p53 regulation; X-ray crystallography
The adaptor protein 14-3-3 binds to and stabilizes the tumor suppressor p53 and enhances its antitumour 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 14-3-3 sigma at a resolution of 1.28 angstrom. 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. Structured summary: MINT-7711943: 14-3-3 sigma (uniprotkb: P31947) and p53 ( uniprotkb: P04637) bind (MI: 0407) by X-ray crystallography ( MI: 0114) MINT-7711931: 14-3-3 sigma ( uniprotkb: P31947) and p53 ( uniprotkb: P04637) bind ( MI: 0407) by isothermal titration calorimetry ( MI: 0065) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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