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| | ==Model of the fiber tail and its interactions with the penton base of human adenovirus by cryo-electron microscopy== | | ==Model of the fiber tail and its interactions with the penton base of human adenovirus by cryo-electron microscopy== |
| - | <StructureSection load='3izo' size='340' side='right'caption='[[3izo]], [[Resolution|resolution]] 3.60Å' scene=''> | + | <SX load='3izo' size='340' side='right' viewer='molstar' caption='[[3izo]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3izo]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_5 Human adenovirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IZO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IZO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3izo]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_adenovirus_5 Human adenovirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IZO FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3iyn|3iyn]]</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=3izo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3izo OCA], [https://pdbe.org/3izo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3izo RCSB], [https://www.ebi.ac.uk/pdbsum/3izo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3izo ProSAT]</span></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=3izo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3izo OCA], [http://pdbe.org/3izo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3izo RCSB], [http://www.ebi.ac.uk/pdbsum/3izo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3izo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [https://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> |
| | <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 3izo" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3izo" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| | [[Category: Human adenovirus 5]] | | [[Category: Human adenovirus 5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Liu, H]] | + | [[Category: Liu H]] |
| - | [[Category: Human adenovirus fiber tail]]
| + | |
| - | [[Category: Pentameric penton base]]
| + | |
| - | [[Category: Trimeric fiber]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
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.[1] [2]
Publication Abstract from PubMed
Adenovirus invades host cells by first binding to host receptors through a trimeric fiber, which contains three domains: a receptor-binding knob domain, a long flexible shaft domain, and a penton base-attachment tail domain. Although the structure of the knob domain associated with a portion of the shaft has been solved by X-ray crystallography, the in situ structure of the fiber in the virion is not known; thus, it remains a mystery how the trimeric fiber attaches to its underlying pentameric penton base. By high-resolution cryo-electron microscopy, we have determined the structure of the human adenovirus type 5- to 3. 6-A resolution and have reported the full atomic models for its capsid proteins, but not for the fiber whose density cannot be directly interpreted due to symmetry mismatch with the penton base. Here, we report the determination of the adenovirus type 5 fiber structure and its mode of attachment to the pentameric penton base by using an integrative approach of multi-resolution filtering, homology modeling, computational simulation of mismatched symmetries, and fitting of atomic models into cryo-electron microscopy density maps. Our structure reveals that the interactions between the trimeric fiber and the pentameric penton base are mediated by a hydrophobic ring on the top surface of the penton base and three flexible tails inserted into three of the five available grooves formed by neighboring subunits of penton base. These interaction sites provide the molecular basis for the symmetry mismatch and can be targeted for optimizing adenovirus for gene therapy applications.
Model of the Trimeric Fiber and Its Interactions with the Pentameric Penton Base of Human Adenovirus by Cryo-electron Microscopy.,Liu H, Wu L, Zhou ZH J Mol Biol. 2010 Dec 10. PMID:21146538[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lyle C, McCormick F. Integrin alphavbeta5 is a primary receptor for adenovirus in CAR-negative cells. Virol J. 2010 Jul 8;7:148. doi: 10.1186/1743-422X-7-148. PMID:20615244 doi:10.1186/1743-422X-7-148
- ↑ Liu H, Jin L, Koh SB, Atanasov I, Schein S, Wu L, Zhou ZH. Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks. Science. 2010 Aug 27;329(5995):1038-43. PMID:20798312 doi:10.1126/science.1187433
- ↑ Liu H, Wu L, Zhou ZH. Model of the Trimeric Fiber and Its Interactions with the Pentameric Penton Base of Human Adenovirus by Cryo-electron Microscopy. J Mol Biol. 2010 Dec 10. PMID:21146538 doi:10.1016/j.jmb.2010.11.043
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