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==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.

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==

Line 13:

[[Category: Human herpesvirus 1]]

[[Category: Single protein]]

[[Category: Abdel-Meguid, S.S.]]

[[Category: Abdel-Meguid, S S.]]

[[Category: Hoog, S.]]

[[Category: Qiu, X.]]

[[Category: Smith, W.W.]]

[[Category: Smith, W W.]]

[[Category: DFP]]

[[Category: hsv2 protease]]

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[[Category: viral protease]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 13: / Line 13: @@
 [[Category: Human herpesvirus 1]]
 [[Category: Single protein]]
-[[Category: Abdel-Meguid, S.S.]]
+[[Category: Abdel-Meguid, S S.]]
 [[Category: Hoog, S.]]
 [[Category: Qiu, X.]]
-[[Category: Smith, W.W.]]
+[[Category: Smith, W W.]]
 [[Category: DFP]]
 [[Category: hsv2 protease]]
@@ Line 22: / Line 22: @@
 [[Category: viral protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:31:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:02 2008''