Table 1.
Binding between ASPP2Ank-SH3 and peptides from Bcl-2 family proteins: SPR studies
| Parent protein | Peptide no. in array | Residues* | Sequence* | Kd, μM |
|---|---|---|---|---|
| Bcl-2 | 2–4 | 7–24 | YDNREIVMKYIHYKLSQR | 1.6 |
| 8 | 45–108† | TESEVVHLTLRQAGDDFSRRYRRD | 10 | |
| 103–120 | RRYRRDFAEMSSQLHLTP | 13 | ||
| Bcl-XL | 42–45 | 6–26 | SQSNRELVVDFLSYKLSQKGY | 23 |
| 103–111 | LRYRRAFSD | 20 | ||
| 50 | 104–123 | RYRRAFSDLTSQLHITPGTA | 26 | |
| 89–111 | AVKQALREAGDEFELRYRRAFSD | No binding | ||
| Bcl-W | 20–22 | 6–28 | PDTRALVADFVGYKLRQKG | Too weak to quantify |
| 54–67 | WETRFRRTFSDLAAQ | Too weak to quantify | ||
| 26–27 | 41–67 | WPLHQAMRAAGDEFETRFRRTFSDLAAQ | Too weak to quantify |
*The combined sequence of overlapping peptides from the same region that bound ASPP2Ank-SH3 in the array. Trp was added at the N terminus of several peptides for UV spectroscopy.
†Bcl-2 45–108 lacks residues 49–88, an unstructured loop that lacks at the crystal structure (23).