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==Crystal Structure of Stabilized GP from Makona Variant of Ebola Virus==
<StructureSection load='6vkm' size='340' side='right'caption='[[6vkm]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VKM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=6vkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vkm OCA], [https://pdbe.org/6vkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vkm RCSB], [https://www.ebi.ac.uk/pdbsum/6vkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vkm ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Ebola virus causes severe hemorrhagic fever, often leading to death in humans. The trimeric fusion glycoprotein (GP) is the sole target for neutralizing antibodies and is the major focus of vaccine development. Soluble GP ectodomains are unstable and mostly monomeric when not fused to a heterologous trimerization domain. Here, we report structure-based designs of Ebola and Marburg GP trimers based on a stabilizing mutation in the hinge loop in refolding region 1 and substitution of a partially buried charge at the interface of the GP1 and GP2 subunits. The combined substitutions (T577P and K588F) substantially increased trimer expression for Ebola GP proteins. We determined the crystal structure of stabilized GP from the Makona Zaire ebolavirus strain without a trimerization domain or complexed ligand. The structure reveals that the stabilized GP adopts the same trimeric prefusion conformation, provides insight into triggering of GP conformational changes, and should inform future filovirus vaccine development.

Structure-Based Design of Prefusion-Stabilized Filovirus Glycoprotein Trimers.,Rutten L, Gilman MSA, Blokland S, Juraszek J, McLellan JS, Langedijk JPM Cell Rep. 2020 Mar 31;30(13):4540-4550.e3. doi: 10.1016/j.celrep.2020.03.025. PMID:32234486<ref>PMID:32234486</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Gilman MSA]]
[[Category: Langedijk JPM]]
[[Category: McLellan JS]]
[[Category: Rutten L]]