Figure 1.

Model of NPC1 Bound to the Primed EBOV GP and Overall Structure of NPC1-C

(A) The full-length EBOV GP was primed by cathepsin L and B in the late endosome, and the highly glycosylated 130 kDa GP1 subunit was cleaved into a 19 kDa GP1, generating a primed form of GP (GPcl). Then, the GPcl binds to the domain C of NPC1 molecule (NPC1-C), which is an endosomal 13-transmembrane protein with three large luminal domains (domains A, C, and I).

(B) Crystal structure of NPC1-C. The helices (α and η) are colored in cyan, the β strands are colored in magenta, and the loops are colored in light pink. The disulfide bonds are colored in yellow. NPC1-C displays a helical core structure surrounded by several β strands with two extended loops.

(C) Topological secondary structure of NPC1-C. Secondary elements are shown as cylinders and arrows for helices and β strands.

See also Figures S1, S2, and S3 and Table S1.