Table 2. Affinities of αE-catenin ABD constructs for actin, determined by co-sedimentation.
KD values and standard deviations for αE-catenin 666–906, 671–906, and 692–906 are the average of three replicate measurements. KD values for the other constructs are the average of two measurements. For αE-catenin 671–906 W859A binding did not reach saturation and therefore only a lower limit for the KD is given. N.D., no detectable binding. Representative binding curves and corresponding gels are shown in Figure 2—figure supplements 2 and 4.
| αE-catenin ABD variant | KD (μM) (SD) |
|---|---|
| 666–906 (full length) | 8.5 (0.7) |
| 671–906 | 2.0 (0.3) |
| 692–906 | 0.7 (0.3) |
| 696–906 | 0.4 (0.05) |
| 699–906 | 0.5 (0.1) |
| 671–872 | 5.0 (0.1) |
| 671–868 | N.D. |
| 671–864 | N.D. |
| 699–868 | 2.8 (0.1) |
| 671–906 W859A | >35 |