View source for 8pag


==Crystal structure of the ectodomain of Norway rat pestivirus E2 glycoprotein==
<StructureSection load='8pag' size='340' side='right'caption='[[8pag]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8pag]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Norway_rat_pestivirus Norway rat pestivirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8PAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PAG 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=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=8pag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8pag OCA], [https://pdbe.org/8pag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8pag RCSB], [https://www.ebi.ac.uk/pdbsum/8pag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8pag ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pestiviruses, within the family Flaviviridae, are economically important viruses of livestock. In recent years, new pestiviruses have been reported in domestic animals and non-cloven-hoofed animals. Among them, atypical porcine pestivirus (APPV) and Norway rat pestivirus (NRPV) have relatively little sequence conservation in their surface glycoprotein E2. Despite E2 being the main target for neutralizing antibodies and necessary for cell attachment and viral fusion, the mechanism of viral entry remains elusive. To gain further insights into the pestivirus E2 mechanism of action and to assess its diversity within the genus, we report X-ray structures of the pestivirus E2 proteins from APPV and NRPV. Despite the highly divergent structures, both are able to dimerize through their C-terminal domain and contain a solvent-exposed beta-hairpin reported to be involved in host receptor binding. Functional analysis of this beta-hairpin in the context of BVDV revealed its ability to rescue viral infectivity.

Structural comparison of typical and atypical E2 pestivirus glycoproteins.,Aitkenhead H, Riedel C, Cowieson N, Rumenapf HT, Stuart DI, El Omari K Structure. 2024 Mar 7;32(3):273-281.e4. doi: 10.1016/j.str.2023.12.003. Epub 2024 , Jan 3. PMID:38176409<ref>PMID:38176409</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8pag" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Norway rat pestivirus]]
[[Category: Aitkenhead H]]
[[Category: EL Omari K]]
[[Category: Stuart DI]]