Protection against Bax | Amino acid | Secondary structure | |||
---|---|---|---|---|---|
Val129 | Met129 | Polarity | Charge | ||
Group I | |||||
WT | Yes | Yes | − | − | β-Sheet 1 |
Group II | |||||
A117V | Yes | Partial | − | − | TM |
V203I | Yes | Partial | − | − | α-Helix C |
T188A | Yes | Partial | + | − | α-Helix B |
E200K | Yes | No | − | + | α-Helix C |
Group III | |||||
D178N | No | Partial | − | + | α-Helix B |
R208H | Partial | No | − | − | α-Helix C |
E211Q | Partial | No | − | + | α-Helix C |
V180I | No | No | − | − | α-Helix B |
E196K | No | No | − | + | Between α-helix B/C |
V210I | No | No | − | − | α-Helix C |
M232R | No | No | + | + | GPI anchor signal |
P238S | No | No | + | − | GPI anchor signal |
Change in the polarity or the charge of the amino acid by 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.