12uv: Difference between revisions

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'''Unreleased structure'''


The entry 12uv is ON HOLD  until Paper Publication
==The AAV2 capsid in complex with IgA-Fab#3-4==
 
<StructureSection load='12uv' size='340' side='right'caption='[[12uv]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
Authors: Zachery, J., Mietzsch, M., McKenna, R.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[12uv]] is a 180 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [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=12UV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=12UV FirstGlance]. <br>
Description: The AAV2 capsid in complex with IgA-Fab#3-4
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.68&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=12uv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=12uv OCA], [https://pdbe.org/12uv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=12uv RCSB], [https://www.ebi.ac.uk/pdbsum/12uv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=12uv ProSAT]</span></td></tr>
[[Category: Mietzsch, M]]
</table>
[[Category: Mckenna, R]]
== Function ==
[[Category: Zachery, J]]
[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>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Adeno-associated virus 2]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: McKenna R]]
[[Category: Mietzsch M]]
[[Category: Zachery J]]