Table 2.
Evaluation of residues involved in RNA recognition.
| RRM1 + 5´-UUAGGUC-3´ | |||
|---|---|---|---|
| RRM1 | Kd (nM) | Affinity loss | N |
| wild-type | 292 ± 17 | 1 | 0.93 ± 0.05 |
| 288 ± 16 | 0.99 ± 0.05 | ||
| F23A | 225 ± 13 | 0.7 | 1.07 ± 0.05 |
| 193 ± 11 | 0.98 ± 0.05 | ||
| D42A | 787 ± 42 | 3 | 0.93 ± 0.05 |
| R55A | >10’000 | >50 | 1 |
| R92A | 1000–5000 | >5 | 1.08 ± 0.05 |
| RRM2 + 5´-UCAGUU-3´ | |||
|---|---|---|---|
| RRM2 | Kd (nM) | Affinity loss | N |
| wild-type | 541 ± 33 | 1 | 1.04 ± 0.05 |
| R140A | 1000–5000 | >2 | 1.07 ± 0.05 |
| Y167F | 513 ± 30 | ~1 | 0.99 ± 0.05 |
| E176Q | 237 ± 15 | 0.4 | 1.01 ± 0.05 |
| M186A | 1630 ± 45 | 3 | 0.96 ± 0.05 |
Values are reported as means ± standard error (S.E.). The uncertainties on the fitted parameters were estimated from the data spread and from the uncertainty of the protein concentration determination (5%). Kd: dissociation constant in nM. Affinity loss: ratio between Kd of the mutant and Kd of the wild-type. N: number of sites.