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- W1979843753 abstract "Human herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2) are responsible for herpes labialis (cold sores) and genital herpes, respectively. They encode a serine protease that is required for viral replication, and represent a viable target for therapeutic intervention. Here, we report the crystal structures of HSV-1 and HSV-2 proteases, the latter in the presence and absence of the covalently bound transition state analog inhibitor diisopropyl phosphate (DIP). The HSV-1 and HSV-2 protease structures show a fold that is neither like chymotrypsin nor like subtilisin, and has been seen only in the recently determined cytomegalovirus (CMV) and varicella-zoster virus (VZV) protease structures. HSV-1 and HSV-2 proteases share high sequence homology and have almost identical three-dimensional structures. However, structural differences are observed with the less homologous CMV protease, offering a structural basis for herpes virus protease ligand specificity. The bound inhibitor identifies the oxyanion hole of these enzymes and defines the active site cavity." @default.
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- W1979843753 date "1997-11-01" @default.
- W1979843753 modified "2023-09-26" @default.
- W1979843753 title "Active Site Cavity of Herpesvirus Proteases Revealed by the Crystal Structure of Herpes Simplex Virus Protease/Inhibitor Complex" @default.
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- W1979843753 doi "https://doi.org/10.1021/bi9712697" @default.
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