Identification of three groups of PrP mutants based on their protection against Bax-mediated cell death in MCF-7 cells
| Protection against Bax | Amino acid | Secondary structure | |||
|---|---|---|---|---|---|
| Val129 | Met129 | Polarity | Charge | ||
| Group I | |||||
| WT | Yes | Yes | − | − | β-Sheet 1 |
| A117V | Yes | Yes | − | − | TM |
| V203I | Yes | Yes | − | − | α-Helix C |
| Group II | |||||
| V180I | Yes | Partial | − | − | α-Helix B |
| E200K | Yes | Partial | − | + | α-Helix C |
| T188A | Yes | Partial | + | − | α-Helix B |
| E196K | Yes | No | − | + | Between α-helix B/C |
| R208H | Yes | No | − | − | α-Helix C |
| Group III | |||||
| E211Q | Partial | Partial | − | + | α-Helix C |
| D178N | Partial | No | − | + | α-Helix B |
| M232R | No | Partial | + | + | GPI anchor signal |
| V210I | No | No | − | − | α-Helix C |
| P238S | No | No | + | − | GPI anchor signal |
Change in the polarity or the charge of the amino acid in the PrP mutation are indicated, using + if there is a change and − if there is no change. The location of the substituted amino acid in the secondary structure of PrP is provided. TM, Transmembrane domain.