Table 2.
Mutants | Mutation position | Surface targeting | oAβ internalization |
---|---|---|---|
R351A | β1 | ━ | ━ |
E360A | β2 | ━ | ━ |
G361P | β2 | ━ | ━ |
R362A | β2 | ━ | ━ |
E364D | β2 | ━ | ━ |
G369S | Turn | ✚ | ✚ |
W371A | β3 | ━ | ━ |
Q385A | α1 | ━ | ━ |
L391A | Loop | ✚ | ✚ |
G395A-Q397A | loop-β4 | ✚ | ✚ |
V399A | β4 | ━ | ━ |
W413A | β5 | ━ | ━ |
F418A | loop | ✚ | ✚ |
C419A | disulfide bond | ━ | ━ |
F420A | loop | ✚ | ✚ |
S424A-S425A | loop | ✚ | ✚ |
R432A | loop | ✚ | ✚ |
R437A | loop | ✚ | ✚ |
R432A-R437A | loop | ✚ | ✚ |
H441R | η2 | ━ | ━ |
D444A | η2-β6 | ━ | ━ |
Mutation position represents the location of mutated residues in the simulated-structure of SRCR domain
✚, mutants are surface-targeted and do not internalize oAβ
━, mutants are not surface-targeted and do not internalize oAβ