6ilj

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==Cryo-EM structure of Echovirus 6 complexed with its attachment receptor CD55 at PH 5.5==
==Cryo-EM structure of Echovirus 6 complexed with its attachment receptor CD55 at PH 5.5==
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<StructureSection load='6ilj' size='340' side='right'caption='[[6ilj]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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<SX load='6ilj' size='340' side='right' viewer='molstar' caption='[[6ilj]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ilj]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Echovirus_e6 Echovirus e6] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ILJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ILJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ilj]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Echovirus_E6 Echovirus E6] 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=6ILJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ILJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SPH:SPHINGOSINE'>SPH</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CD55, CR, DAF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SPH:SPHINGOSINE'>SPH</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ilj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ilj OCA], [http://pdbe.org/6ilj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ilj RCSB], [http://www.ebi.ac.uk/pdbsum/6ilj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ilj ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ilj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ilj OCA], [https://pdbe.org/6ilj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ilj RCSB], [https://www.ebi.ac.uk/pdbsum/6ilj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ilj ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[[http://www.uniprot.org/uniprot/DAF_HUMAN DAF_HUMAN]] This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade.<ref>PMID:7525274</ref>
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== Publication Abstract from PubMed ==
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Enterovirus B (EV-B), a major proportion of the genus Enterovirus in the family Picornaviridae, is the causative agent of severe human infectious diseases. Although cellular receptors for coxsackievirus B in EV-B have been identified, receptors mediating virus entry, especially the uncoating process of echovirus and other EV-B remain obscure. Here, we found that human neonatal Fc receptor (FcRn) is the uncoating receptor for major EV-B. FcRn binds to the virus particles in the "canyon" through its FCGRT subunit. By obtaining multiple cryo-electron microscopy structures at different stages of virus entry at atomic or near-atomic resolution, we deciphered the underlying mechanisms of enterovirus attachment and uncoating. These structures revealed that different from the attachment receptor CD55, binding of FcRn to the virions induces efficient release of "pocket factor" under acidic conditions and initiates the conformational changes in viral particle, providing a structural basis for understanding the mechanisms of enterovirus entry.
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Human Neonatal Fc Receptor Is the Cellular Uncoating Receptor for Enterovirus B.,Zhao X, Zhang G, Liu S, Chen X, Peng R, Dai L, Qu X, Li S, Song H, Gao Z, Yuan P, Liu Z, Li C, Shang Z, Li Y, Zhang M, Qi J, Wang H, Du N, Wu Y, Bi Y, Gao S, Shi Y, Yan J, Zhang Y, Xie Z, Wei W, Gao GF Cell. 2019 May 30;177(6):1553-1565.e16. doi: 10.1016/j.cell.2019.04.035. Epub, 2019 May 16. PMID:31104841<ref>PMID:31104841</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6ilj" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[CD55|CD55]]
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Echovirus e6]]
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[[Category: Echovirus E6]]
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gao, G F]]
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[[Category: Gao GF]]
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[[Category: Liu, S]]
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[[Category: Liu S]]
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[[Category: Peng, R]]
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[[Category: Peng R]]
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[[Category: Zhao, X]]
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[[Category: Zhao X]]
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[[Category: Cd55]]
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[[Category: Cryo-em]]
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[[Category: Echovirus 6]]
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[[Category: Virus]]
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[[Category: Virus-receptor complex]]
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Current revision

Cryo-EM structure of Echovirus 6 complexed with its attachment receptor CD55 at PH 5.5

6ilj, resolution 3.60Å

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