Journal
PROTEIN SCIENCE
Volume 17, Issue 10, Pages 1663-1670Publisher
WILEY
DOI: 10.1110/ps.035527.108
Keywords
p53; S100 proteins; tetramerization; negative regulatory domain; protein-protein interactions
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Funding
- Medical Research Council-UK
- MRC [MC_U105474168] Funding Source: UKRI
- Medical Research Council [MC_U105474168] Funding Source: researchfish
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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.
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