Members of the S100 family bind p53 in two distinct ways.
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.
Fernandez-Fernandez
Maria Rosario
MR
Centre for Protein Engineering, Medical Research Council, Cambridge University, Cambridge CB2 0QH, United Kingdom.
Rutherford
Trevor J
TJ
Fersht
Alan R
AR
D000595:Amino Acid Sequence; D006801:Humans; D008969:Molecular Sequence Data; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000071999:S100 Calcium-Binding Protein A4; D009418:S100 Proteins / Q000737:chemistry / Q000378:metabolism*; D016415:Sequence Alignment; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D011994:Recombinant Proteins; D000071999:S100 Calcium-Binding Protein A4; D009418:S100 Proteins; D016159:Tumor Suppressor Protein p53; C077591:S100A4 protein, human; C072337:S100A11 protein, human