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. 2019 Feb 8;17(2):e3000141. doi: 10.1371/journal.pbio.3000141

Fig 5. Dissimilar CCS membrane interaction surfaces.

Fig 5

(A) The structure of domain II β-barrel loops I, IV, and VII are not conserved among yeast and human CCS orthologues. (B) Coulombic charge representation showing differing putative hCCS and yCCS domain II membrane-interacting surfaces. (C) Liposome-binding assay showing how the concerted effect of all three hCCS domains facilitate membrane association (S7C and S7D Fig). hCCS dimer affinity, domain I electropositivity, and complexation with SOD1 all effect lipid association. Mean ± SEM, n = 5. CCS, copper chaperone for SOD1; hCCS, human copper chaperone for SOD1; SOD1, superoxide dismutase-1; yCCS, yeast copper chaperone for SOD1.