Crystal Structure of Varicella-Zoster Virus Protease

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- angstrom resolution. The VZV protease is essential for the life cycle of t...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1997-04, Vol.94 (7), p.2874-2879
Main Authors: Qiu, Xiayang, Janson, Cheryl A., Culp, Jeffrey S., Richardson, Susan B., Debouck, Christine, Smith, Ward W., Abdel-Meguid, Sherin S.
Format: Article
Language:English
Subjects:
Active sites
Amino Acid Sequence
Atoms
Biochemistry
Biological Sciences
Catalysis
Crystal structure
Crystallography, X-Ray
Crystals
Cytomegalovirus
Dimers
Herpesvirus 3, Human - enzymology
Human herpesvirus 1
Molecular Sequence Data
Protein Conformation
Proteins
Sequence Homology, Amino Acid
Serine Endopeptidases - chemistry
Serine Endopeptidases - metabolism
Substrate Specificity
Varicella zoster encephalitis
Varicella-zoster virus
Viral morphology
Viruses
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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- angstrom 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.94.7.2874