TABLE 1.
Parameters describing the stability and structure of EphA2 unliganded dimers
Kdiss is the dissociation constant (receptors/μm2); ΔG is the dimerization free energy; Ẽ is the intrinsic FRET efficiency; and d is the calculated distance between the fluorescent proteins in the EphA2 dimers. Kdiss and Ẽ are determined from the fit of the dimerization model to the FRET data, and the uncertainties are the 95% confidence intervals from the fit. ΔG and d are calculated using Equations 1 and 2, respectively.
| Kdiss | ΔG | Ẽ | d | |
|---|---|---|---|---|
| receptors/μm2 | kcal/mol | Å | ||
| Wild-type EphA2 | 210 ± 50 | −5.0 ± 0.2 | 0.67 ± 0.03 | 48 ± 1 |
| L223R | 310 ± 60 | −4.8 ± 0.1 | 0.65 ± 0.03 | 49 ± 1 |
| L223R/L254R | 320 ± 100 | −5.1 ± 0.1 | 0.46 ± 0.03 | 56 ± 1 |
| L223R/L254R/V255R | 1200 ± 250 | −4.0 ± 0.2 | 0.72 ± 0.04 | 47 ± 1 |