Table 1.
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.