3iyn

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{{Large structure}}
==3.6-Angstrom cryoEM structure of human adenovirus type 5==
==3.6-Angstrom cryoEM structure of human adenovirus type 5==
<StructureSection load='3iyn' size='340' side='right' caption='[[3iyn]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
<StructureSection load='3iyn' size='340' side='right' caption='[[3iyn]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3iyn]] is a 20 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_5 Human adenovirus 5]. The December 2010 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Adenovirus'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2010_12 10.2210/rcsb_pdb/mom_2010_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IYN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3iyn]] is a 20 chain structure with sequence from [http://en.wikipedia.org/wiki/Ade05 Ade05]. The December 2010 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Adenovirus'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2010_12 10.2210/rcsb_pdb/mom_2010_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IYN 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=3iyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iyn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3iyn RCSB], [http://www.ebi.ac.uk/pdbsum/3iyn PDBsum]</span></td></tr>
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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=3iyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iyn OCA], [http://pdbe.org/3iyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3iyn RCSB], [http://www.ebi.ac.uk/pdbsum/3iyn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3iyn ProSAT]</span></td></tr>
</table>
</table>
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{{Large structure}}
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HEX8_ADE05 HEX8_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/HEX_ADE05 HEX_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/PEN3_ADE05 PEN3_ADE05]] Major capsid protein that self-associates to form penton base pentamers, each in the shape of a pentagon, situated at the 12 verteces 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 shedded concomitant with virion acidification in the endosome.<ref>PMID:20615244</ref> <ref>PMID:20798312</ref>
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[[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/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/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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3iyn ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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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 3iyn" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ade05]]
[[Category: Adenovirus]]
[[Category: Adenovirus]]
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[[Category: Human adenovirus 5]]
 
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Atanasov, I]]
[[Category: Atanasov, I]]

Revision as of 02:51, 5 August 2016

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3.6-Angstrom cryoEM structure of human adenovirus type 5

3iyn, resolution 3.60Å

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