1vzv
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STRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASE
OverviewOverview
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.
About this StructureAbout this Structure
1VZV is a Single protein structure of sequence from Varicella-zoster virus (isolate 40a2). Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of varicella-zoster virus protease., Qiu X, Janson CA, Culp JS, Richardson SB, Debouck C, Smith WW, Abdel-Meguid SS, Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):2874-9. PMID:9096314
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