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This Article ACCEPTED PREPRINT Full Text (PDF) All Versions of this Article: ps.035527.108v1 17/10/1663    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Google Scholar Articles by Fernandez-Fernandez, M. R. Articles by Fersht, A. R PubMed PubMed Citation Articles by Fernandez-Fernandez, M. R. Articles by Fersht, A. R Social Bookmarking                   What's this?

Members of the S100 family bind p53 in two distinct ways

¹ Centre for Protein Engineering;
² Cambridge

(RECEIVED April 1, 2008; ACCEPTED May 27, 2008)

p53 binds to some members of the S100 family (S100B, S100A4, S100A2 and S100A1). We previously showed that both S100B and S100A4 bind to p53 tetramerization domain, and consequently control its oligomerization state, but only S100B binds to the C-terminal negative regulatory domain. Here, we found new binding partners for p53 within the S100 family (S100A6 and S100A11). Moreover, we show that binding to p53 tetramerization domain seems to be a general feature of the S100 family while the binding to the negative regulatory domain is a particular characteristic of only a few members.

Keywords: Specificity; Structure/function studies; NMR Spectroscopy; Fluorescence; Calorimetry; Protein-protein interactions

³ E-mail: arf25{at}cam.ac.uk

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