4cwu
From Proteopedia
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==CRYSTAL STRUCTURE DERIVED MODELS OF ADENOVIRUS CEMENT PROTEINS AT 3.8A== | ==CRYSTAL STRUCTURE DERIVED MODELS OF ADENOVIRUS CEMENT PROTEINS AT 3.8A== | ||
<StructureSection load='4cwu' size='340' side='right' caption='[[4cwu]], [[Resolution|resolution]] 3.80Å' scene=''> | <StructureSection load='4cwu' size='340' side='right' caption='[[4cwu]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
| - | </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://www.rcsb.org/pdb/explore.do?structureId=4cwu RCSB], [http://www.ebi.ac.uk/pdbsum/4cwu PDBsum]</span></td></tr> | + | </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> |
</table> | </table> | ||
| + | {{Large structure}} | ||
== Function == | == Function == | ||
[[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). | [[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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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 4cwu" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 05:24, 5 August 2016
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CRYSTAL STRUCTURE DERIVED MODELS OF ADENOVIRUS CEMENT PROTEINS AT 3.8A
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