6ill
From Proteopedia
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<SX load='6ill' size='340' side='right' viewer='molstar' caption='[[6ill]], [[Resolution|resolution]] 3.80Å' scene=''> | <SX load='6ill' size='340' side='right' viewer='molstar' caption='[[6ill]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6ill]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6ill]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Echovirus_E6 Echovirus E6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ILL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ILL 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]] 3.8Å</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=6ill FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ill OCA], [https://pdbe.org/6ill PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ill RCSB], [https://www.ebi.ac.uk/pdbsum/6ill PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ill ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | + | ==See Also== | |
| - | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |
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__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
| - | [[Category: Echovirus | + | [[Category: Echovirus E6]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Gao | + | [[Category: Gao GF]] |
| - | [[Category: Liu | + | [[Category: Liu S]] |
| - | [[Category: Peng | + | [[Category: Peng R]] |
| - | [[Category: Zhao | + | [[Category: Zhao X]] |
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Current revision
Cryo-EM structure of Echovirus 6 complexed with its uncoating receptor FcRn at PH 5.5
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Categories: Echovirus E6 | Large Structures | Gao GF | Liu S | Peng R | Zhao X
