TABLE 1.
Properties of serpins used in this study
| Serpin | Sequence of inhibitory regiona | Interaction with granzyme B (ka [M−1 s−1]) |
|---|---|---|
| PI-9 | ‥320VEVNEEGTEAAAASSCFVVAE=CCMESGPRFCADHPFL‥ | (1.7 ± 0.3) × 106 |
| PI9E340D | ‥320VEVNEEGTEAAAASSCFVVAD=CCMESGPRFCADHPFL‥ | (1.4 ± 0.3) × 104 |
| PI9E340A | ‥320VEVNEEGTEAAAASSCFVVAA=CCMESGPRFCADHPFL‥ | (5.8 ± 0.6) × 103 |
| PI9T327R | ‥320VEVNEEGREAAAASSCFVVAE=CCMESGPRFCADHPFL‥ | (8.7 ± 1.0) × 102 |
| CrmA | ‥284IDVNEEYTEAAAAT-CALVAD=CASTVTNEFCADHPFI‥ | 2.9 × 105b |
a
The sequences of PI-9 and CrmA were taken from references 45 and 33, respectively. Only the portions comprising the hinge and reactive centers of each serpin are shown. A space introduced to optimize sequence alignment is indicated by a single dash. Mutated residues are indicated in boldface. The P1-P1′ bond is indicated by a double dash.
b
Value taken from reference 32.