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PDBsum entry 1vzv
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Serine protease
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PDB id
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1vzv
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References listed in PDB file
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Key reference
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Title
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Crystal structure of varicella-Zoster virus protease.
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Authors
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X.Qiu,
C.A.Janson,
J.S.Culp,
S.B.Richardson,
C.Debouck,
W.W.Smith,
S.S.Abdel-Meguid.
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Ref.
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Proc Natl Acad Sci U S A, 1997,
94,
2874-2879.
[DOI no: ]
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PubMed id
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Abstract
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Varicella-zoster virus (VZV), an alpha-herpes virus, is the causative agent of
chickenpox, shingles, and postherpetic neuralgia. The three-dimensional crystal
structure of the serine protease from VZV has been determined at 3.0-A
resolution. The VZV protease is essential for the life cycle of the virus and is
a potential target for therapeutic intervention. The structure reveals an
overall fold that is similar to that recently reported for the serine protease
from cytomegalovirus (CMV), a herpes virus of the beta subfamily. The VZV
protease structure provides further evidence to support the finding that herpes
virus proteases have a fold and active site distinct from other serine
proteases. The VZV protease catalytic triad consists of a serine and two
histidines. The distal histidine is proposed to properly orient the proximal
histidine. The identification of an alpha-helical segment in the VZV protease
that was mostly disordered in the CMV protease provides a better definition of
the postulated active site cavity and reveals an elastase-like S' region.
Structural differences between the VZV and CMV proteases also suggest potential
differences in their oligomerization states.
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Figure 4.
Fig. 4. The catalytic residues (A) in the omit F[o]  F[c] map
contoured at 3  . (B) VZV
protease (red) compared with CMV (blue) and trypsin (yellow).
Dashed lines connects the catalytic triad of the VZV protease.
Only CMV numbering is used.
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Figure 5.
Fig. 5. Molecular surface of the VZV protease looking into
the postulated substrate binding groove. The surface is
color-coded by electrostatic potentials (blue for positive and
red for negative) calculated with the program GRASP (28).
Modeled is the Ala-Ser cleavage site. The red arrow indicates
the position of the scissile^ bond.
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Secondary reference #1
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Title
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Unique fold and active site in cytomegalovirus protease.
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Authors
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X.Qiu,
J.S.Culp,
A.G.Dilella,
B.Hellmig,
S.S.Hoog,
C.A.Janson,
W.W.Smith,
S.S.Abdel-Meguid.
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Ref.
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Nature, 1996,
383,
275-279.
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PubMed id
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