Structure of the p53 C-terminus bound to 14-3-3: Implications for stabilization of the p53 tetramer

B. Schumacher, J. Mondry, P. Thiel, M. Weyand, C. Ottmann

Research output: Contribution to journalArticleAcademicpeer-review

66 Citations (Scopus)

Abstract

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
Original languageEnglish
Pages (from-to)1433-1448
Number of pages6
JournalFEBS Letters
Volume584
Issue number8
DOIs
Publication statusPublished - 2010

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