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Table 2 Summary of the surface targeting and oAβ internalization of mutants in SRCR domain of human SR-AI

From: Identifying N-linked glycan moiety and motifs in the cysteine-rich domain critical for N-glycosylation and intracellular trafficking of SR-AI and MARCO

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
  1. Mutation position represents the location of mutated residues in the simulated-structure of SRCR domain
  2. ✚, mutants are surface-targeted and do not internalize oAβ
  3. ━, mutants are not surface-targeted and do not internalize oAβ