1at3 | pdb_00001at3
HERPES SIMPLEX VIRUS TYPE II PROTEASE
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| 1at3, resolution 2.5Å | |||||||||||||
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| Sites: | ACT | ||||||||||||
| Ligands: | DFP | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1AT3 is a Single protein structure of sequence from Human herpesvirus 2. Full crystallographic information is available from OCA.
Reference
Active site cavity of herpesvirus proteases revealed by the crystal structure of herpes simplex virus protease/inhibitor complex., Hoog SS, Smith WW, Qiu X, Janson CA, Hellmig B, McQueney MS, O'Donnell K, O'Shannessy D, DiLella AG, Debouck C, Abdel-Meguid SS, Biochemistry. 1997 Nov 18;36(46):14023-9. PMID:9369473
Page seeded by OCA on Sun Mar 30 18:46:57 2008
