Members of the S100 family bind p53 in two distinct ways

被引：69

作者：

Fernandez-Fernandez, Maria Rosario ^{[1
]}

Rutherford, Trevor J. ^{[1
]}

Fersht, Alan R. ^{[1
]}

机构：

[1] Univ Cambridge, Dept Chem, Ctr Prot Engn, MRC, Cambridge CB2 1EW, England

来源：

PROTEIN SCIENCE | 2008年 / 17卷 / 10期

基金：

英国医学研究理事会;

关键词：

p53; S100; proteins; tetramerization; negative regulatory domain; protein-protein interactions;

D O I：

10.1110/ps.035527.108

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1663 / 1670

页数：8

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