View source for 9bop


==A broadly-neutralizing antibody against Ebolavirus glycoprotein that can potentiate the breadth and neutralization potency of other anti-glycoprotein antibodies==
<StructureSection load='9bop' size='340' side='right'caption='[[9bop]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9bop]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Ebolavirus Ebolavirus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BOP 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]] 3&#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=MAN:ALPHA-D-MANNOSE'>MAN</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=9bop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bop OCA], [https://pdbe.org/9bop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bop RCSB], [https://www.ebi.ac.uk/pdbsum/9bop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bop ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A8G0KJC2_9MONO A0A8G0KJC2_9MONO] Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in GP2, releasing the fusion hydrophobic peptide.[ARBA:ARBA00060272]  Functions as a decoy for anti-GP1,2 antibodies thereby contributing to viral immune evasion. Interacts and activates host macrophages and dendritic cells inducing up-regulation of cytokine transcription. This effect is mediated throught activation of host TLR4.[ARBA:ARBA00058844]
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</StructureSection>
[[Category: Ebolavirus]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Balaram A]]
[[Category: Callaway H]]
[[Category: Donnellan FR]]
[[Category: Draper SJ]]
[[Category: Halfmann P]]
[[Category: Hariharan C]]
[[Category: Hastie K]]
[[Category: Hui S]]
[[Category: Lightwood DJ]]
[[Category: Muller-Krauter H]]
[[Category: O'Dowd V]]
[[Category: Parekh D]]
[[Category: Parvate A]]
[[Category: Rayaprolu V]]
[[Category: Rijal P]]
[[Category: Saphire EO]]
[[Category: Shaffer K]]
[[Category: Shimanski L]]
[[Category: Stecker T]]
[[Category: Townsend AR]]