9cbn: Difference between revisions

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'''Unreleased structure'''


The entry 9cbn is ON HOLD until Paper Publication
==HAstV1 spike in complex with neutralizing Fabs 3H4 and 3B4==
 
<StructureSection load='9cbn' size='340' side='right'caption='[[9cbn]], [[Resolution|resolution]] 3.33&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[9cbn]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_astrovirus_1 Human astrovirus 1] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CBN FirstGlance]. <br>
Description:  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.33&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=9cbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cbn OCA], [https://pdbe.org/9cbn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cbn RCSB], [https://www.ebi.ac.uk/pdbsum/9cbn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cbn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAPSD_HASV1 CAPSD_HASV1] The capsid polyprotein VP90 self-assembles and undergoes a proteolytic cleavage by host caspases to yield the immature VP70 virion.[UniProtKB:Q9IFX1]  The immature virion is composed of 180 VP70 subunits with 90 dimeric spikes and displays a T=3 icosahedral symmetry (By similarity). During maturation, VP70 undergoes a loss of 60 peripentonal spikes, which likely plays an important role in viral infectivity (By similarity).[UniProtKB:Q9IFX1] Self-assembles to form an icosahedral capsid with a T=3 symmetry, about 43 nm in diameter (PubMed:26656707). This forms contains only 30 spikes located on the icosahedral 2-fold axes (PubMed:26656707).<ref>PMID:26656707</ref>  VP25 and VP27 Forms the spikes at the surface of the virion (PubMed:26656707). This forms contains only 30 spikes located on the icosahedral 2-fold axes (PubMed:26656707). Plays a role in the attachment to target host cell (Probable). This attachment induces virion internalization through clathrin-dependent endocytosis (By similarity).[UniProtKB:Q9IFX1]<ref>PMID:26656707</ref>  VP25 and VP27 Forms the spikes at the surface of the virion (PubMed:26656707). This forms contains only 30 spikes located on the icosahedral 2-fold axes (PubMed:26656707). Plays a role in the attachment to target host cell (PubMed:33396308). This attachment induces virion internalization through clathrin-dependent endocytosis (By similarity).[UniProtKB:Q9IFX1]<ref>PMID:26656707</ref> <ref>PMID:33396308</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human astrovirus 1]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Balasco Serrao VH]]
[[Category: DuBois RM]]
[[Category: Lanning S]]

Latest revision as of 09:31, 25 December 2024

HAstV1 spike in complex with neutralizing Fabs 3H4 and 3B4

9cbn, resolution 3.33Å

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