Fig. 4: Detailed structural interactions between the SUDV RBS and Loop 2 of hNPC1-C.
From: Cryo-EM structure of Sudan ebolavirus glycoprotein complexed with its human endosomal receptor NPC1
A Interactions between Ala148/Lys155 in the EBOV RBS and Loop 2 of hNPC1-C. B Interactions between Pro148/Lys155 in the SUDV RBS and Loop 2 of hNPC1-C. A dotted line in (A) indicates a long-range salt bridge, which is absent in (B) due to the greater distance. The double arrow in (B) represents a hydrophobic interaction that cannot form in (A) because of the larger distance. C Interactions between Val79/Val141 in the EBOV RBS and Loop 2 of hNPC1-C. D Interactions between Ile79/Ala141 in the SUDV RBS and Loop 2 of hNPC1-C. In (C), red double arrows indicate unfavorable interactions between a polar functional group and hydrophobic functional groups. In (D), the distance is sufficient to alleviate these unfavorable interactions, and the black double arrow highlights a favorable hydrophobic interaction.
