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==== | ==E30 F-particle in complex with CD55== | ||
<StructureSection load='7c9w' size='340' side='right'caption='[[7c9w]]' scene=''> | <StructureSection load='7c9w' size='340' side='right'caption='[[7c9w]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[7c9w]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Echovirus_E30 Echovirus E30] 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=7C9W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C9W FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=SPH:SPHINGOSINE'>SPH</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=7c9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c9w OCA], [https://pdbe.org/7c9w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c9w RCSB], [https://www.ebi.ac.uk/pdbsum/7c9w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c9w ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Receptor usage that determines cell tropism and drives viral classification closely correlates with the virus structure. Enterovirus B (EV-B) consists of several subgroups according to receptor usage, among which echovirus 30 (E30), a leading causative agent for human aseptic meningitis, utilizes FcRn as an uncoating receptor. However, receptors for many EVs remain unknown. Here we analyzed the atomic structures of E30 mature virion, empty- and A-particles, which reveals serotype-specific epitopes and striking conformational differences between the subgroups within EV-Bs. Of these, the VP1 BC loop markedly distinguishes E30 from other EV-Bs, indicative of a role as a structural marker for EV-B. By obtaining cryo-electron microscopy structures of E30 in complex with its receptor FcRn and CD55 and comparing its homologs, we deciphered the underlying molecular basis for receptor recognition. Together with experimentally derived viral receptor identifications, we developed a structure-based in silico algorithm to inform a rational prediction for EV receptor usage. | |||
Structures of Echovirus 30 in complex with its receptors inform a rational prediction for enterovirus receptor usage.,Wang K, Zhu L, Sun Y, Li M, Zhao X, Cui L, Zhang L, Gao GF, Zhai W, Zhu F, Rao Z, Wang X Nat Commun. 2020 Sep 4;11(1):4421. doi: 10.1038/s41467-020-18251-9. PMID:32887891<ref>PMID:32887891</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7c9w" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[CD55|CD55]] | |||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Echovirus E30]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Z | [[Category: Cui L]] | ||
[[Category: Gao G]] | |||
[[Category: Li M]] | |||
[[Category: Rao Z]] | |||
[[Category: Sun Y]] | |||
[[Category: Wang K]] | |||
[[Category: Wang X]] | |||
[[Category: Zhai W]] | |||
[[Category: Zhang L]] | |||
[[Category: Zhao X]] | |||
[[Category: Zhu F]] | |||
[[Category: Zhu L]] | |||
Latest revision as of 11:38, 17 October 2024
E30 F-particle in complex with CD55E30 F-particle in complex with CD55
Structural highlights
Publication Abstract from PubMedReceptor usage that determines cell tropism and drives viral classification closely correlates with the virus structure. Enterovirus B (EV-B) consists of several subgroups according to receptor usage, among which echovirus 30 (E30), a leading causative agent for human aseptic meningitis, utilizes FcRn as an uncoating receptor. However, receptors for many EVs remain unknown. Here we analyzed the atomic structures of E30 mature virion, empty- and A-particles, which reveals serotype-specific epitopes and striking conformational differences between the subgroups within EV-Bs. Of these, the VP1 BC loop markedly distinguishes E30 from other EV-Bs, indicative of a role as a structural marker for EV-B. By obtaining cryo-electron microscopy structures of E30 in complex with its receptor FcRn and CD55 and comparing its homologs, we deciphered the underlying molecular basis for receptor recognition. Together with experimentally derived viral receptor identifications, we developed a structure-based in silico algorithm to inform a rational prediction for EV receptor usage. Structures of Echovirus 30 in complex with its receptors inform a rational prediction for enterovirus receptor usage.,Wang K, Zhu L, Sun Y, Li M, Zhao X, Cui L, Zhang L, Gao GF, Zhai W, Zhu F, Rao Z, Wang X Nat Commun. 2020 Sep 4;11(1):4421. doi: 10.1038/s41467-020-18251-9. PMID:32887891[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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