1at3
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Human herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2) are | + | 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== | ==About this Structure== | ||
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[[Category: Human herpesvirus 1]] | [[Category: Human herpesvirus 1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Abdel-Meguid, S | + | [[Category: Abdel-Meguid, S S.]] |
[[Category: Hoog, S.]] | [[Category: Hoog, S.]] | ||
[[Category: Qiu, X.]] | [[Category: Qiu, X.]] | ||
| - | [[Category: Smith, W | + | [[Category: Smith, W W.]] |
[[Category: DFP]] | [[Category: DFP]] | ||
[[Category: hsv2 protease]] | [[Category: hsv2 protease]] | ||
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[[Category: viral protease]] | [[Category: viral protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:02 2008'' |
Revision as of 09:48, 21 February 2008
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HERPES SIMPLEX VIRUS TYPE II PROTEASE
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 1 with as ligand. Known structural/functional Site: . 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
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