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| - | {{Large structure}}
| + | #REDIRECT [[6cgv]] This PDB entry is obsolete and replaced by 6cgv |
| - | ==CRYSTAL STRUCTURE DERIVED MODELS OF ADENOVIRUS CEMENT PROTEINS AT 3.8A==
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| - | <StructureSection load='4cwu' size='340' side='right' caption='[[4cwu]], [[Resolution|resolution]] 3.80Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[4cwu]] is a 23 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vsz 1vsz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CWU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CWU FirstGlance]. <br>
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| - | </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=4cwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cwu OCA], [http://pdbe.org/4cwu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cwu RCSB], [http://www.ebi.ac.uk/pdbsum/4cwu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cwu ProSAT]</span></td></tr>
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| - | </table>
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| - | {{Large structure}}
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| - | == Function ==
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| - | [[http://www.uniprot.org/uniprot/CAP6_ADE05 CAP6_ADE05]] Pre-protein VI: During virus assembly, promotes hexon trimers nuclear import through nuclear pore complexes via an importin alpha/beta-dependent mechanism. By analogy to herpesviruses capsid assembly, might act as a scaffold protein to promote the formation of the icosahedral capsid.<ref>PMID:14633984</ref> <ref>PMID:15681401</ref> <ref>PMID:20333243</ref> <ref>PMID:20409568</ref> <ref>PMID:21209115</ref> Endosome lysis protein: Structural component of the virion that provides increased stability to the particle shell through its interaction with the core-capsid bridging protein. Fibers shedding during virus entry into host cell allows the endosome lysis protein to be exposed as a membrane-lytic peptide. Exhibits pH-independent membrane fragmentation activity and probably mediates viral rapid escape from host endosome via organellar membrane lysis. It is not clear if it then remains partially associated with the capsid and involved in the intracellular microtubule-dependent transport of capsid to the nucleus, or if it is lost during endosomal penetration.<ref>PMID:14633984</ref> <ref>PMID:15681401</ref> <ref>PMID:20333243</ref> <ref>PMID:20409568</ref> <ref>PMID:21209115</ref> Protease cofactor: Cofactor that activates the viral protease. Binds to viral protease in a 1:1 ratio.<ref>PMID:14633984</ref> <ref>PMID:15681401</ref> <ref>PMID:20333243</ref> <ref>PMID:20409568</ref> <ref>PMID:21209115</ref> [[http://www.uniprot.org/uniprot/CAP9_ADE05 CAP9_ADE05]] Structural component of the virion that presumably stabilizes the groups of hexons but is dispensable for assembly. During virus entry, recruits the anterograde motor kinesin-1 to the capsid docked at the nuclear pore complex thereby subjecting the docked capsid to a pulling force. The resulting tension leads to capsid disruption, dispersion of capsid fragments toward cell periphery and eventually viral DNA entry into the host nucleus. [[http://www.uniprot.org/uniprot/CAPSH_ADE05 CAPSH_ADE05]] Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein (By similarity). Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus. [[http://www.uniprot.org/uniprot/CAP3_ADE05 CAP3_ADE05]] Structural component of the virion that is likely to participate in vertex stabilization and genome packaging. Stabilizes vertices by tethering the penton bases to neighboring peripentonal hexons. Lashes peripentonal hexons to the neighboring hexons thanks to its interaction with hexon-linking protein. As the virus enters the host cell, capsid vertex proteins are shed concomitant with virion acidification in the endosome. During virus assembly, seems to play a role in packaging of viral DNA via its interaction with packaging protein 3.<ref>PMID:21632753</ref> <ref>PMID:20798312</ref> [[http://www.uniprot.org/uniprot/CAP8_ADE05 CAP8_ADE05]] Hexon-linking protein: Structural component of the virion that lashes peripentonal hexons to the hexons situated in the facets thanks to its interaction with the capsid vertex protein. Also binds together hexons of different facets. [[http://www.uniprot.org/uniprot/CAPSP_ADE05 CAPSP_ADE05]] Major capsid protein that self-associates to form penton base pentamers, each in the shape of a pentagon, situated at the 12 vertices of the pseudo T=25 capsid. Involved in virus secondary attachment to host cell after initial attachment by the fiber protein. Binds host integrin heterodimer ITGAV-ITGB5 (alphaV-beta5) thereby triggering clathrin-mediated endocytosis of virions. Mediates initial virus attachment to CXADR-negative cells. Binding to integrins ITGAV-ITGB5 also seems to induce macropinocytosis uptake of the virus. As the virus enters the host cell, penton proteins are shed concomitant with virion acidification in the endosome.<ref>PMID:20615244</ref> <ref>PMID:20798312</ref> [[http://www.uniprot.org/uniprot/CORE5_ADE05 CORE5_ADE05]] Associates loosely with the viral DNA to form an outer shell around the nucleoprotein-DNA complex and links it with the capsid by binding the endosome lysis protein. Dissociates from the viral genome during entry. Might be involved in nuclear assembly of the viral particles through its association with NPM1/nucleophosmin (By similarity).
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Adenovirus cement proteins play crucial roles in virion assembly, disassembly, cell entry, and infection. Based on a refined crystal structure of the adenovirus virion at 3.8-A resolution, we have determined the structures of all of the cement proteins (IIIa, VI, VIII, and IX) and their organization in two distinct layers. We have significantly revised the recent cryoelectron microscopy models for proteins IIIa and IX and show that both are located on the capsid exterior. Together, the cement proteins exclusively stabilize the hexon shell, thus rendering penton vertices the weakest links of the adenovirus capsid. We describe, for the first time to our knowledge, the structure of protein VI, a key membrane-lytic molecule, and unveil its associations with VIII and core protein V, which together glue peripentonal hexons beneath the vertex region and connect them to the rest of the capsid on the interior. Following virion maturation, the cleaved N-terminal propeptide of VI is observed, reaching deep into the peripentonal hexon cavity, detached from the membrane-lytic domain, so that the latter can be released. Our results thus provide the molecular basis for the requirement of maturation cleavage of protein VI. This process is essential for untethering and release of the membrane-lytic region, which is known to mediate endosome rupture and delivery of partially disassembled virions into the host cell cytoplasm.
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| - | Structures and organization of adenovirus cement proteins provide insights into the role of capsid maturation in virus entry and infection.,Reddy VS, Nemerow GR Proc Natl Acad Sci U S A. 2014 Jul 28. pii: 201408462. PMID:25071205<ref>PMID:25071205</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4cwu" style="background-color:#fffaf0;"></div>
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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: Nemerow, G R]]
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| - | [[Category: Reddy, V S]]
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| - | [[Category: Adenovirus]]
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| - | [[Category: Cement protein]]
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| - | [[Category: Protein vi]]
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| - | [[Category: Virus]]
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