6u0v

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(New page: '''Unreleased structure''' The entry 6u0v is ON HOLD Authors: Agbandje-Mckenna, M., Bennett, A. Description: Atomic-Resolution Cryo-EM Structure of AAV2 VLP [[Category: Unreleased Stru...)
Current revision (09:28, 20 March 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6u0v is ON HOLD
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==Atomic-Resolution Cryo-EM Structure of AAV2 VLP==
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<StructureSection load='6u0v' size='340' side='right'caption='[[6u0v]], [[Resolution|resolution]] 3.02&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6u0v]] is a 60 chain structure with sequence from [https://en.wikipedia.org/wiki/Adeno-associated_virus_2 Adeno-associated virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6U0V FirstGlance]. <br>
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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]] 3.02&#8491;</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=6u0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u0v OCA], [https://pdbe.org/6u0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6u0v RCSB], [https://www.ebi.ac.uk/pdbsum/6u0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6u0v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAPSD_AAV2S CAPSD_AAV2S] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of three size variants of the capsid protein VP1, VP2 and VP3 which differ in their N-terminus. The capsid encapsulates the genomic ssDNA. Binds to host cell heparan sulfate and uses host ITGA5-ITGB1 as coreceptor on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptor also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and putative nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus.<ref>PMID:10684294</ref> <ref>PMID:11961250</ref> <ref>PMID:16940508</ref> <ref>PMID:9445046</ref>
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Authors: Agbandje-Mckenna, M., Bennett, A.
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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Description: Atomic-Resolution Cryo-EM Structure of AAV2 VLP
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Bennett, A]]
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__TOC__
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[[Category: Agbandje-Mckenna, M]]
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</StructureSection>
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[[Category: Adeno-associated virus 2]]
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[[Category: Large Structures]]
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[[Category: Agbandje-Mckenna M]]
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[[Category: Bennett A]]

Current revision

Atomic-Resolution Cryo-EM Structure of AAV2 VLP

PDB ID 6u0v

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