TABLE 2.
Binding characteristics, stability data, and in vivo localization of Pyd PDZ2 mutants
| Pyd PDZ2 | KDapp PtdIns(4,5)P2, composite liposomes | KD LKLPPEERLI | ΔΔGD-N | In vivo localizationa |
|---|---|---|---|---|
| μm | μm | kcal/mol | ||
| F194W | 0.40 ± 0.05 | 220 ± 20 | Membrane | |
| F194W/K179A | 2.9 ± 0.4 | 100 ± 30 | 0.54 ± 0.05 | Diffuse |
| F194W/K180A | 4 ± 1 | 300 ± 60 | 1.23 ± 0.04 | Diffuse |
| F194W/K199A | 2.9 ± 0.8 | 190 ± 50 | 1.59 ± 0.05 | Diffuse |
| F194W/R201A | 0.6 ± 0.1 | 231 ± 13 | −0.61 ± 0.02 | Membrane |
| F194W/K232A | 3.5 ± 0.4 | 177 ± 12 | 3.2 ± 0.3 | Diffuse |
| F194W/K235A | 2.4 ± 0.4 | 176 ± 20 | −0.16 ± 0.01 | Diffuse |
| F194W/K236A | 3.6 ± 0.6 | >1000 | 1.14 ± 0.03 | Diffuse |
| F194W/K242A | 14 ± 4 | >1000 | −0.19 ± 0.01 | Diffuse |
| F194W/R244A | 1.4 ± 0.2 | 520 ± 100 | −1.9 ± 0.2 | Membrane |
a The mutations were introduced in the background of wild-type eYFP-Pyd PDZ2.