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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1997-5-8
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-1312713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-1654435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-3018124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-3640709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-7559392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-7795518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-7983728,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-8066444,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-8175677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-8189508,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-8230459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-8244978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-8254766,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-8382296,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-8611517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-8631772,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-8797829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-8805706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-8805707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9096314-8805708
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
94
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2874-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9096314-Amino Acid Sequence,
pubmed-meshheading:9096314-Catalysis,
pubmed-meshheading:9096314-Crystallography, X-Ray,
pubmed-meshheading:9096314-Herpesvirus 3, Human,
pubmed-meshheading:9096314-Molecular Sequence Data,
pubmed-meshheading:9096314-Protein Conformation,
pubmed-meshheading:9096314-Sequence Homology, Amino Acid,
pubmed-meshheading:9096314-Serine Endopeptidases,
pubmed-meshheading:9096314-Substrate Specificity
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pubmed:year |
1997
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pubmed:articleTitle |
Crystal structure of varicella-zoster virus protease.
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pubmed:affiliation |
Department of Macromolecular Sciences, SmithKline Beecham Pharmaceuticals, King of Prussia, PA 19406, USA.
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pubmed:publicationType |
Journal Article
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