1at3: Difference between revisions

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.

1AT3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1] with DFP as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: ACT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AT3 OCA].  

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