Format

Send to

Choose Destination
FEBS Lett. 2010 Apr 16;584(8):1443-8. doi: 10.1016/j.febslet.2010.02.065. Epub 2010 Mar 3.

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

Author information

1
Chemical Genomics Centre of the Max-Planck-Society, Dortmund, Germany.

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.

PMID:
20206173
DOI:
10.1016/j.febslet.2010.02.065
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center