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Potent and selective inhibition of pathogenic viruses by engineered ubiquitin variants

Fig 3

Structural basis for UbV inhibition of CCHFV OTU.

(A-C) Crystal structure of (A) the CCHFV OTU-CC.2 complex, (B) the CCHFV OTU-CC.4 complex, and (C) the CCHFV OTU-Ub.wt complex (PDB ID: 3PT2). OTU domains are shown as surface representations, and coloured in cyan, light cyan and slate for the OTU-CC.2, -CC.4 and–Ub.wt complexes, respectively. CC.2, CC.4 and Ub.wt are shown as tubes and coloured in yellow, magenta and orange, respectively. (D) Overlay of the CCHFV OTU-CC.2, CC.4 and–Ub.wt structures showing interactions between CCHFV OTU and CC.2 or CC.4 residue Tyr68 or Ub.wt residue His68. UbV and Ub.wt residues are shown as sticks and labeled in regular font. CCHFV OTU residues are shown as sticks and labeled in italics with asterisks. (E) Close up of interactions between the C-terminus of CC.2 and CCHFV OTU. (F) Close up of interactions between the C-terminus of CC.4 and CCHFV OTU. (G) Close up of interactions between the C-terminus of Ub.wt and the active site of CCHFV OTU. Figures were generated using PyMOL [61].

Fig 3

doi: https://doi.org/10.1371/journal.ppat.1006372.g003