4adj

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==Crystal structure of the Rubella virus glycoprotein E1 in its post-fusion form crystallized in presence of 1mM of calcium acetate==
==Crystal structure of the Rubella virus glycoprotein E1 in its post-fusion form crystallized in presence of 1mM of calcium acetate==
<StructureSection load='4adj' size='340' side='right' caption='[[4adj]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
<StructureSection load='4adj' size='340' side='right' caption='[[4adj]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4adj]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Rubella_virus Rubella virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ADJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4adj]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Rubv Rubv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ADJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4adg|4adg]], [[4adi|4adi]], [[4b3v|4b3v]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4adg|4adg]], [[4adi|4adi]], [[4b3v|4b3v]]</td></tr>
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<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=4adj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4adj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4adj RCSB], [http://www.ebi.ac.uk/pdbsum/4adj PDBsum]</span></td></tr>
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<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=4adj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4adj OCA], [http://pdbe.org/4adj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4adj RCSB], [http://www.ebi.ac.uk/pdbsum/4adj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4adj ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/POLS_RUBVM POLS_RUBVM]] Capsid protein interacts with genomic RNA and assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion, but this interaction seems not to be important for its biological function. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells. E2 envelope glycoprotein is responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein. E1 envelope glycoprotein is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion (By similarity). E1 cytoplasmic tail modulates virus release, and the tyrosines residues are critical for this function.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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 4adj" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Rubella virus]]
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[[Category: Rubv]]
[[Category: Barba-Spaeth, G]]
[[Category: Barba-Spaeth, G]]
[[Category: Dubois, R M]]
[[Category: Dubois, R M]]

Revision as of 19:12, 10 December 2016

Crystal structure of the Rubella virus glycoprotein E1 in its post-fusion form crystallized in presence of 1mM of calcium acetate

4adj, resolution 1.94Å

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