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PDBsum entry 1at3
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Serine protease
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PDB id
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1at3
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Active site cavity of herpesvirus proteases revealed by the crystal structure of herpes simplex virus protease/inhibitor complex.
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Authors
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S.S.Hoog,
W.W.Smith,
X.Qiu,
C.A.Janson,
B.Hellmig,
M.S.Mcqueney,
K.O'Donnell,
D.O'Shannessy,
A.G.Dilella,
C.Debouck,
S.S.Abdel-Meguid.
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Ref.
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Biochemistry, 1997,
36,
14023-14029.
[DOI no: ]
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PubMed id
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Abstract
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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.
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