TABLE 3.
KD values for the binding of RAP D1D2 and mutants located in D2 to LRP1
Experiments were performed in duplicate. Boldface entries identify large changes in KD1 relative to WT D1D2.
| Protein | KD1 fold change | KD2 fold change | % complex IIa |
|---|---|---|---|
| RAP D1D2 | 1.0 | 1.0 | 87 |
| RAP D1D2 K93A | 5.5 | 0.8 | 76 |
| RAP D1D2 K94A | 7.2 | 0.7 | 65 |
| RAP D1D2 K93A/K94A | 23.6 | 0.9 | 70 |
| RAP D1D2 K119A | 3.5 | 0.3 | 58 |
| RAP D1D2 K123A | 9.4 | 0.8 | 80 |
| RAP D1D2 K125A | 4.5 | 0.3 | 61 |
| RAP D1D2 K119A/K123A | 1.2 | 0.4 | 50 |
| RAP D1D2 K123A/K125A | 33.8 | 0.4 | 71 |
| RAP D1D2 129A | 3.3 | 0.8 | 75 |
| RAP D1D2 137A | 2.9 | 0.4 | 63 |
| RAP D1D2 K146A | 4.0 | 0.8 | 80 |
| RAP D1D2 K148A | 2.3 | 0.5 | 57 |
| RAP D1D2 K146A/K148A | 2.1 | 0.4 | 71 |
| RAP D1D2 K179A | 1.0 | 0.4 | 67 |
| RAP D1D2 K191A | 2.3 | 0.3 | 47 |
| RAP D1D2 K193A | 7.5 | 0.3 | 58 |
| RAP D1D2 K191A/K193A | 3.8 | 2.9 | 50 |
| RAP D1D2 K148A/K193A | 1.3 | 0.7 | 72 |
a Percent of complex II present in the reaction with 1.6 nm D1D2 is shown.