1vzv: Difference between revisions

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 ==STRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASE==
-<StructureSection load='1vzv' size='340' side='right' caption='[[1vzv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+<StructureSection load='1vzv' size='340' side='right'caption='[[1vzv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1vzv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hhv-3 Hhv-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>
+<table><tr><td colspan='2'>[[1vzv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_3 Human alphaherpesvirus 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 [https://proteopedia.org/fgij/fg.htm?mol=1VZV FirstGlance]. <br>
-</td></tr><tr id='resources'><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://pdbe.org/1vzv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vzv RCSB], [http://www.ebi.ac.uk/pdbsum/1vzv PDBsum]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzv OCA], [https://pdbe.org/1vzv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vzv RCSB], [https://www.ebi.ac.uk/pdbsum/1vzv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vzv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SCAF_VZVD SCAF_VZVD]] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein 40 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein 40 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein 40. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity).  Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity).  Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein 40. Multimerizes in the nucleus such as protein 40 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).
+[https://www.uniprot.org/uniprot/SCAF_VZVD SCAF_VZVD] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein 40 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein 40 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein 40. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity).  Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity).  Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein 40. Multimerizes in the nucleus such as protein 40 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).
 == 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>
+     <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].
+</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/main_output.php?pdb_ID=1vzv 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1vzv" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Virus protease|Virus protease]]
+*[[Virus protease 3D structures|Virus protease 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Hhv-3]]
+[[Category: Human alphaherpesvirus 3]]
-[[Category: Abdel-Meguid, S S]]
+[[Category: Large Structures]]
-[[Category: Culp, J S]]
+[[Category: Abdel-Meguid SS]]
-[[Category: Debouck, C]]
+[[Category: Culp JS]]
-[[Category: Jason, C A]]
+[[Category: Debouck C]]
-[[Category: Qiu, X]]
+[[Category: Jason CA]]
-[[Category: Richardson, S B]]
+[[Category: Qiu X]]
-[[Category: Smith, W W]]
+[[Category: Richardson SB]]
-[[Category: Coat protein]]
+[[Category: Smith WW]]
-[[Category: Hydrolase]]
-[[Category: Serine protease]]
-[[Category: Varicella-zoster virus]]
-[[Category: Viral protease]]