Table 1.
ssDNA binding affinity and cooperativity of APOBEC3A and interface mutants. The hill coefficient (nH) is expected to be 1 for non-cooperative binding and 2 for cooperative binding by a dimer. Note: A3A refers to the inactive variant E72A. See also Supplemental Table 1 for oligomer sequences.
| KD [nM] | KD relative to polyT_1C |
nH | |
|---|---|---|---|
| A3A vs TTC | 77 ± 3 | 1.4 | 2.1 ± 0.1 |
| A3A vs TCC | 114 ± 4 | 2.0 | 2.5 ± 0.2 |
| A3A vs CCC | 100 ± 4 | 1.8 | 2.1 ± 0.2 |
| A3A vs polyT_1C | 56 ± 2 | 1.0 | 1.8 ± 0.1 |
| A3A vs polyT_2C | 44 ± 2 | 0.8 | 1.6 ± 0.1 |
| A3A vs polyT_3C | 59 ± 2 | 1.1 | 2.2 ± 0.1 |
| A3A vs polyT_4C | 61 ± 3 | 1.1 | 1.7 ± 0.1 |
| A3A vs polyT | 502 ± 27 | 9.0 | 0.96 ± 0.04 |
| A3A vs polyT_1U | 434 ± 35 | 7.8 | 0.80 ± 0.04 |
| A3A H11A vs polyT_1C | 855 ± 311 | 15.3 | 0.7 ± 0.1 |
| A3A H16A vs polyT_1C | 584 ± 92 | 10.4 | 1.2 ± 0.2 |
| A3A K30E vs polyT_1C | 284 ± 20 | 5.1 | 1.2 ± 0.1 |
| A3A H56A vs polyT_1C | 86 ± 13 | 1.5 | 0.9 ± 0.1 |
| A3A E72Q vs polyT_1C | 26 ± 2 | 0.5 | 1.8 ± 0.1 |
| A3A E72Q vs polyT_1U | 296 ± 125 | 5.3 | 1.0 ± 0.2 |
| A3A E72Q vs polyT | 205 ± 20 | 3.7 | 1.4 ± 0.2 |