1vzv: Difference between revisions
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[[Image: | ==STRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASE== | ||
<StructureSection load='1vzv' size='340' side='right' caption='[[1vzv]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1vzv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_3 Human herpesvirus 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VZV FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vzv RCSB], [http://www.ebi.ac.uk/pdbsum/1vzv PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vz/1vzv_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:9096314</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Virus protease|Virus protease]] | *[[Virus protease|Virus protease]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Human herpesvirus 3]] | [[Category: Human herpesvirus 3]] | ||
[[Category: Abdel-Meguid, S S.]] | [[Category: Abdel-Meguid, S S.]] |
Revision as of 23:00, 28 September 2014
STRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASESTRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASE
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedVaricella-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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