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• W2022357516 startingPage "2874" @default.
• W2022357516 abstract "Varicella-zoster virus (VZV), an α-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-Å 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 β 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 α-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." @default.
• W2022357516 created "2016-06-24" @default.
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• W2022357516 date "1997-04-01" @default.
• W2022357516 modified "2023-09-27" @default.
• W2022357516 title "Crystal structure of varicella-zoster virus protease" @default.
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• W2022357516 doi "https://doi.org/10.1073/pnas.94.7.2874" @default.
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