Table 1.
Solvent accessibility, secondary structure, and frequency of the residues selected for mutation
| Residue position* | Location† | Solvent accessibility of side chain in wild type, %‡ | Frequency of residue in p53 family§
|
|
|---|---|---|---|---|
| human p53 | variant p53 | |||
| Q104 (P)(H) | End of N terminus | 56.7 | 0.2 | 0.4 (0.15) |
| A129 (S)(D)(E) | Turn between S2 and S2′ | 77.3 | 0.1 | 0.3 (0.15) (0.15) |
| M133(L) | S2′ | 0.7 | 0.15 | 0.8 |
| D148(S)(E) | Turn between S3 and S4 | 71.1 | 0.43 | 0.24 (0.1) |
| T150(P) | Turn between S3 and S4 | 64.3 | 0.43 | 0.52 |
| Q165(K) | L2 | 43.4 | 0.14 | 0.86 |
| Q167(E) | L2 | 71.2 | 0.43 | 0.52 |
| R174(K) | L2 | 57.5 | 0.81 | 0.19 |
| C182(S) | L2 | 35.3 | 0.55 | 0.36 |
| L201(P) | Turn between S5 and S6 | 89.5 | 0.73 | 0.14 |
| V203(A) | Turn between S5 and S6 | 0.7 | 0.18 | 0.68 |
| L206(S) | S6 | 47.8 | 0.55 | 0.1 |
| D228(E) | Turn between S7 and S8 | 77.5 | 0.50 | 0.5 |
| Y236(F) | End of S8 | 0.4 | 0.57 | 0.43 |
| N239(Y) | L3 | 34.5 | 0.91 | 0 |
| S260(P) | Turn between S9 and S10 | 64.9 | 0.61 | 0.22 |
| N268(D) | S10 | 13.8 | 0.52 | 0.1 |
*
The position according to the sequence of the human 53 protein and the Protein Data Bank (6, 7). The residues in brackets are those of the mutants; in bold are cancer mutations.
†
Location of the residue according to the crystal structure of the protein in the Protein Data Bank (6).
‡
Solvent accessibility (in percent), defined as solvent accessible surface area of the amino acid residue in its parent protein calculated by whatif (19), divided by the solvent accessibility of that residue in an extended Ala-X-Ala peptide.
§
Relative frequency of occurrence as calculated from the alignment of 23 p53 proteins by using human p53 as the reference (7).