Fig. 3: Detailed structural interactions between the SUDV RBS and Loop 1 of hNPC1-C.
From: Cryo-EM structure of Sudan ebolavirus glycoprotein complexed with its human endosomal receptor NPC1
A A significant conformational change in Loop 1 of hNPC1-C is observed when bound to SUDV compared to EBOV. This shift involves Loop 1 moving 6.3 Å away from the RBS, driven by the presence of Q142 in the SUDV RBS. B Detailed interactions between the EBOV RBS and Loop 1 of hNPC1-C. C Detailed interactions between the SUDV RBS and Loop 1 of hNPC1-C. Double arrows in (B) indicate hydrophobic stacking interactions, whereas in (C), the distances are too great to support such hydrophobic stacking interactions.
