Fig. 5: The extensive hydrogen-bond and electrostatic interaction network between ISG15 C-terminus and SARS-CoV-2 PLpro. | Nature Communications

Fig. 5: The extensive hydrogen-bond and electrostatic interaction network between ISG15 C-terminus and SARS-CoV-2 PLpro.

From: The complex structure of GRL0617 and SARS-CoV-2 PLpro reveals a hot spot for antiviral drug discovery

Fig. 5

a The complex structure of human ISG15 C-UBL domain and SARS-CoV-2 PLpro (PDB 6XA9 [https://doi.org/10.2210/pdb6xa9/pdb]). b Close-up view for interactions of the C-terminus of ISG15 (green) with PLpro (marine), sidechain interactions in black dashed lines, and backbone interactions in red dashed lines. c Surface model showing the superposition of the C-terminus of ISG15 on apo-PLpro (PDB 6W9C [https://doi.org/10.2210/pdb6w9c/pdb]). d Surface model showing the C-terminus of ISG15 in PLpro (PDB 6XA9 [https://doi.org/10.2210/pdb6xa9/pdb]). e Cartoon model showing the shift of BL2 loop from the apo-state (orange) to bound state (marine), a distance of 4.5 Å was labeled for the shifting of sidechain η-OH of Y268 in PLpro.

Back to article page