View source for 9ay1


==Cryo-EM structure of SINV/EEEV in complex with a potently neutralizing human antibody IgG EEEV-373==
<StructureSection load='9ay1' size='340' side='right'caption='[[9ay1]], [[Resolution|resolution]] 4.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ay1]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Eastern_equine_encephalitis_virus Eastern equine encephalitis virus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9AY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9AY1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.6&#8491;</td></tr>
<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=9ay1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ay1 OCA], [https://pdbe.org/9ay1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ay1 RCSB], [https://www.ebi.ac.uk/pdbsum/9ay1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ay1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/W8R5E4_EEEV W8R5E4_EEEV] 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 endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane. Fusion is optimal at levels of about 1 molecule of cholesterol per 2 molecules of phospholipids, and is specific for sterols containing a 3-beta-hydroxyl group.[ARBA:ARBA00055183]  Constitutive membrane protein involved in virus glycoprotein processing, cell permeabilization, and the budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level. This leads to cytoplasmic calcium elevation. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Present in low amount in virions, about 3% compared to viral glycoproteins.[ARBA:ARBA00037269]  Provides the signal sequence for the translocation of the precursor of protein E3/E2 to the host endoplasmic reticulum. Furin-cleaved E3 remains associated with spike glycoprotein E1 and mediates pH protection of the latter during the transport via the secretory pathway. After virion release from the host cell, the assembly protein E3 is gradually released in the extracellular space.[ARBA:ARBA00037518]
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</StructureSection>
[[Category: Eastern equine encephalitis virus]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bandyopadhyay A]]
[[Category: Klose T]]
[[Category: Kuhn RJ]]