Table 1. Interaction of wild-type S100A4 with ezrin constructs*.
| Trp fluorescence | FP | Competitive FP | |
|---|---|---|---|
| N-ERMAD | 2.2 ± 0.2 (3.9 ± 0.2) | – | 1.1 ± 0.2 |
| F2 lobe | < 0.1 (0.17 ± 0.07) | – | 0.12 ± 0.08 |
| C-ERMAD | – | 3.4 ± 0.1 | 5.3 ± 0.5 |
| C-ERMAD516–560 | – | 8.4 ± 0.8 | 27.6 ± 3.1 |
| C-ERMADT567D | – | 2.7 ± 0.1 | – |
| Ezrin | 174.6 ± 23.3 | – | 92.1 ± 6.9 |
| EzrinT567D | 157.6 ± 38.6 | – | 72.2 ±5.0 |
*Values represent the equilibrium dissociation constants (Kd, mean ± SEM) in μM. The Kd values determined in stopped-flow experiment are shown in parentheses. For direct FP measurements, fluorescently-labeled C-ERMAD derivatives were used. In the competitive FP assays Fl-NMIIA1908-1937 was applied as a tracer.