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| | <SX load='4v4u' size='340' side='right' viewer='molstar' caption='[[4v4u]], [[Resolution|resolution]] 10.00Å' scene=''> | | <SX load='4v4u' size='340' side='right' viewer='molstar' caption='[[4v4u]], [[Resolution|resolution]] 10.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4v4u]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/Ade02 Ade02] and [http://en.wikipedia.org/wiki/Ade05 Ade05]. 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 [http://proteopedia.org/fgij/fg.htm?mol=4V4U FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1x9p|1x9p]], [[1x9t|1x9t]]</td></tr> | + | </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=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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4v4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4u OCA], [http://pdbe.org/4v4u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v4u RCSB], [http://www.ebi.ac.uk/pdbsum/4v4u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v4u ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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. | + | [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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| | </div> | | </div> |
| | <div class="pdbe-citations 4v4u" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4v4u" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Ade02]] | + | [[Category: Human adenovirus 2]] |
| - | [[Category: Ade05]] | + | [[Category: Human adenovirus 5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Conway, J F]] | + | [[Category: Conway JF]] |
| - | [[Category: Cusack, S]] | + | [[Category: Cusack S]] |
| - | [[Category: Fabry, C M.S]] | + | [[Category: Fabry CMS]] |
| - | [[Category: Rosa-Calatrava, M]] | + | [[Category: Rosa-Calatrava M]] |
| - | [[Category: Ruigrok, R W.H]] | + | [[Category: Ruigrok RWH]] |
| - | [[Category: Schoehn, G]] | + | [[Category: Schoehn G]] |
| - | [[Category: Zubieta, C]] | + | [[Category: Zubieta C]] |
| - | [[Category: Adenovirus]]
| + | |
| - | [[Category: Minor capsid protein]]
| + | |
| - | [[Category: Quasi atomic]]
| + | |
| - | [[Category: Virus]]
| + | |
| Structural highlights
Function
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.
Publication Abstract from PubMed
Adenoviruses infect a wide range of vertebrates including humans. Their icosahedral capsids are composed of three major proteins: the trimeric hexon forms the facets and the penton, a noncovalent complex of the pentameric penton base and trimeric fibre proteins, is located at the 12 capsid vertices. Several proteins (IIIa, VI, VIII and IX) stabilise the capsid. We have obtained a 10 A resolution map of the human adenovirus 5 by image analysis from cryo-electron micrographs (cryoEMs). This map, in combination with the X-ray structures of the penton base and hexon, was used to build a quasi-atomic model of the arrangement of the two major capsid components and to analyse the hexon-hexon and hexon-penton interactions. The secondary proteins, notably VIII, were located by comparing cryoEM maps of native and pIX deletion mutant virions. Minor proteins IX and IIIa are located on the outside of the capsid, whereas protein VIII is organised with a T=2 lattice on the inner face of the capsid. The capsid organisation is compared with the known X-ray structure of bacteriophage PRD1.
A quasi-atomic model of human adenovirus type 5 capsid.,Fabry CM, Rosa-Calatrava M, Conway JF, Zubieta C, Cusack S, Ruigrok RW, Schoehn G EMBO J. 2005 May 4;24(9):1645-54. Epub 2005 Apr 21. PMID:15861131[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fabry CM, Rosa-Calatrava M, Conway JF, Zubieta C, Cusack S, Ruigrok RW, Schoehn G. A quasi-atomic model of human adenovirus type 5 capsid. EMBO J. 2005 May 4;24(9):1645-54. Epub 2005 Apr 21. PMID:15861131
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