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Members of the S100 family bind p53 in two distinct ways.


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

SUBMITTER: Fernandez-Fernandez MR 

PROVIDER: S-EPMC2548378 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature

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Members of the S100 family bind p53 in two distinct ways.

Fernandez-Fernandez Maria Rosario MR   Rutherford Trevor J TJ   Fersht Alan R AR  

Protein science : a publication of the Protein Society 20080811 10


p53 binds to some members of the S100 family (S100B, S100A4, S100A2, and S100A1). We previously showed that both S100B and S100A4 bind to the p53 tetramerization domain, and consequently control its oligomerization state, but only S100B binds to the C-terminal negative regulatory domain (NRD). Here, we investigate other binding partners for p53 within the S100 family (S100A6 and S100A11), and show that binding to the p53 tetramerization domain seems to be a general feature of the S100 family, wh  ...[more]

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