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4v4u

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(New page: ==The quasi-atomic model of Human Adenovirus type 5 capsid== <StructureSection load='4v4u' size='340' side='right' caption='4v4u, resolution 10.00&Aring;' scene=''> == S...)
Current revision (11:26, 9 May 2024) (edit) (undo)
 
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==The quasi-atomic model of Human Adenovirus type 5 capsid==
==The quasi-atomic model of Human Adenovirus type 5 capsid==
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<StructureSection load='4v4u' size='340' side='right' caption='[[4v4u]], [[Resolution|resolution]] 10.00&Aring;' scene=''>
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<SX load='4v4u' size='340' side='right' viewer='molstar' caption='[[4v4u]], [[Resolution|resolution]] 10.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4v4u]] is a 22 chain structure. This structure supersedes the now removed PDB entries and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bvi 2bvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V4U FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4v4u]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_adenovirus_2 Human adenovirus 2] and [https://en.wikipedia.org/wiki/Human_adenovirus_5 Human adenovirus 5]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bld 2bld] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bvi 2bvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V4U FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bld|2bld]], [[2bvi|2bvi]], [[1x9p|1x9p]], [[1x9t|1x9t]]</td></tr>
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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]] 10&#8491;</td></tr>
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<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=4v4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v4u RCSB], [http://www.ebi.ac.uk/pdbsum/4v4u PDBsum]</span></td></tr>
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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=4v4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4u OCA], [https://pdbe.org/4v4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v4u RCSB], [https://www.ebi.ac.uk/pdbsum/4v4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v4u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CAPSP_ADE02 CAPSP_ADE02]] 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:12221069</ref> <ref>PMID:20615244</ref> <ref>PMID:20798312</ref> [[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.
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[https://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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4v4u" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Conway, J F]]
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[[Category: Human adenovirus 2]]
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[[Category: Cusack, S]]
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[[Category: Human adenovirus 5]]
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[[Category: Fabry, C M.S]]
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[[Category: Large Structures]]
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[[Category: Rosa-Calatrava, M]]
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[[Category: Conway JF]]
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[[Category: Ruigrok, R W.H]]
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[[Category: Cusack S]]
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[[Category: Schoehn, G]]
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[[Category: Fabry CMS]]
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[[Category: Zubieta, C]]
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[[Category: Rosa-Calatrava M]]
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[[Category: Adenovirus]]
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[[Category: Ruigrok RWH]]
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[[Category: Minor capsid protein]]
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[[Category: Schoehn G]]
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[[Category: Quasi atomic]]
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[[Category: Zubieta C]]
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[[Category: Virus]]
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Current revision

The quasi-atomic model of Human Adenovirus type 5 capsid

4v4u, resolution 10.00Å

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