View source for 5xea


==Structure of Thogoto virus envelope glycoprotein==
<StructureSection load='5xea' size='340' side='right'caption='[[5xea]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xea]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thogoto_virus_(isolate_SiAr_126) Thogoto virus (isolate SiAr 126)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XEA 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]] 2.093&#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=5xea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xea OCA], [https://pdbe.org/5xea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xea RCSB], [https://www.ebi.ac.uk/pdbsum/5xea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xea ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ENV_THOGV ENV_THOGV] Possible role in endocytotic fusion events during infection.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Thogotoviruses are emerging tick-borne zoonotic orthomyxoviruses infecting both humans and domestic animals with severe clinical consequences. These viruses utilize a single-envelope glycoprotein (Gp) to facilitate their entry into host cells. Here, we present the Gp structures of Thogoto and Dhori viruses, both of which are members of the Thogotovirus genus in the family Orthomyxoviridae These structures, determined in the postfusion conformation, identified them as class III viral fusion proteins. It is intriguing that the Gp structures are similar to the envelope protein of baculovirus, although sharing a low sequence identity of approximately 28%. Detailed structural and phylogenic analyses demonstrated that these Gps originated from a common ancestor. Among the structures, domain I is the most conserved region, particularly the fusion loops. Domain II showed the highest variability among different viruses, which might be related to their distinct host tropism. These findings increase our understanding of the divergent evolution processes of various orthomyxoviruses and indicate potential targets for developing antiviral therapeutics by intercepting virus entry.

Structures of human-infecting Thogotovirus fusogens support a common ancestor with insect baculovirus.,Peng R, Zhang S, Cui Y, Shi Y, Gao GF, Qi J Proc Natl Acad Sci U S A. 2017 Oct 17;114(42):E8905-E8912. doi:, 10.1073/pnas.1706125114. Epub 2017 Oct 4. PMID:29073031<ref>PMID:29073031</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xea" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Gao GF]]
[[Category: Peng R]]
[[Category: Qi J]]
[[Category: Shi Y]]