8xa0

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Current revision (06:16, 4 December 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8xa0 is ON HOLD
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==penton capsomer of the VZV C-capsid==
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<StructureSection load='8xa0' size='340' side='right'caption='[[8xa0]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
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Authors: Nan, W., Lei, C., Xiangxi, W.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8xa0]] is a 13 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=8XA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XA0 FirstGlance]. <br>
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Description: penton capsomer of the VZV C-capsid
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8xa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xa0 OCA], [https://pdbe.org/8xa0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xa0 RCSB], [https://www.ebi.ac.uk/pdbsum/8xa0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xa0 ProSAT]</span></td></tr>
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[[Category: Nan, W]]
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</table>
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[[Category: Xiangxi, W]]
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== Function ==
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[[Category: Lei, C]]
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[https://www.uniprot.org/uniprot/LTP_HHV11 LTP_HHV11] Large tegument protein that plays multiple roles in the viral cycle. During viral entry, remains associated with the capsid while most of the tegument is detached and participates in the capsid transport toward the host nucleus. Plays a role in the routing of the capsid at the nuclear pore complex and subsequent uncoating. Within the host nucleus, acts as a deneddylase and promotes the degradation of nuclear CRLs (cullin-RING ubiquitin ligases) and thereby stabilizes nuclear CRL substrates, while cytoplasmic CRLs remain unaffected. These modifications prevent host cell cycle S-phase progression and create a favorable environment allowing efficient viral genome replication. Participates later in the secondary envelopment of capsids. Indeed, plays a linker role for the association of the outer viral tegument to the capsids together with the inner tegument protein.[HAMAP-Rule:MF_04044]<ref>PMID:16306630</ref> <ref>PMID:18216103</ref> <ref>PMID:18495763</ref> <ref>PMID:18971278</ref> <ref>PMID:19923173</ref> <ref>PMID:20190741</ref> <ref>PMID:22345483</ref> <ref>PMID:22718835</ref> <ref>PMID:23186167</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Human alphaherpesvirus 3]]
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[[Category: Large Structures]]
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[[Category: Lei C]]
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[[Category: Nan W]]
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[[Category: Xiangxi W]]

Current revision

penton capsomer of the VZV C-capsid

PDB ID 8xa0

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