5bno: Difference between revisions
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''' | ==Crystal structure of human enterovirus D68 in complex with 6'SLN== | ||
<StructureSection load='5bno' size='340' side='right' caption='[[5bno]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5bno]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterovirus_d68 Enterovirus d68]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BNO FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4U1:(6R)-5-(ACETYLAMINO)-3,5-DIDEOXY-6-[(1R,2R)-1,2,3-TRIHYDROXYPROPYL]-BETA-L-THREO-HEX-2-ULOPYRANONOSYL-(2- 6)-BETA-D-GALACTOPYRANOSYL-(1- 4)-2-(ACETYLAMINO)-2-DEOXY-BETA-D-GLUCOPYRANOSE'>4U1</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bnn|5bnn]], [[5bnp|5bnp]]</td></tr> | |||
<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=5bno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bno OCA], [http://pdbe.org/5bno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bno RCSB], [http://www.ebi.ac.uk/pdbsum/5bno PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human enterovirus D68 (EV-D68) is a causative agent of childhood respiratory diseases and has now emerged as a global public health threat. Nevertheless, knowledge of the tissue tropism and pathogenesis of EV-D68 has been hindered by a lack of studies on the receptor-mediated EV-D68 entry into host cells. Here we demonstrate that cell surface sialic acid is essential for EV-D68 to bind to and infect susceptible cells. Crystal structures of EV-D68 in complex with sialylated glycan receptor analogues show that they bind into the 'canyon' on the virus surface. The sialic acid receptor induces a cascade of conformational changes in the virus to eject a fatty-acid-like molecule that regulates the stability of the virus. Thus, virus binding to a sialic acid receptor and to immunoglobulin-like receptors used by most other enteroviruses share a conserved mechanism for priming viral uncoating and facilitating cell entry. | |||
Sialic acid-dependent cell entry of human enterovirus D68.,Liu Y, Sheng J, Baggen J, Meng G, Xiao C, Thibaut HJ, van Kuppeveld FJ, Rossmann MG Nat Commun. 2015 Nov 13;6:8865. doi: 10.1038/ncomms9865. PMID:26563423<ref>PMID:26563423</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5bno" style="background-color:#fffaf0;"></div> | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Enterovirus d68]] | |||
[[Category: Liu, Y]] | [[Category: Liu, Y]] | ||
[[Category: Meng, G]] | [[Category: Meng, G]] | ||
[[Category: Rossmann, M | [[Category: Rossmann, M G]] | ||
[[Category: Sheng, J]] | [[Category: Sheng, J]] | ||
[[Category: Xiao, C]] | |||
[[Category: Beta jelly roll]] | |||
[[Category: Capsid]] | |||
[[Category: Enterovirus]] | |||
[[Category: Receptor]] | |||
[[Category: Virus]] | |||
Revision as of 22:22, 30 November 2015
Crystal structure of human enterovirus D68 in complex with 6'SLNCrystal structure of human enterovirus D68 in complex with 6'SLN
Structural highlights
Publication Abstract from PubMedHuman enterovirus D68 (EV-D68) is a causative agent of childhood respiratory diseases and has now emerged as a global public health threat. Nevertheless, knowledge of the tissue tropism and pathogenesis of EV-D68 has been hindered by a lack of studies on the receptor-mediated EV-D68 entry into host cells. Here we demonstrate that cell surface sialic acid is essential for EV-D68 to bind to and infect susceptible cells. Crystal structures of EV-D68 in complex with sialylated glycan receptor analogues show that they bind into the 'canyon' on the virus surface. The sialic acid receptor induces a cascade of conformational changes in the virus to eject a fatty-acid-like molecule that regulates the stability of the virus. Thus, virus binding to a sialic acid receptor and to immunoglobulin-like receptors used by most other enteroviruses share a conserved mechanism for priming viral uncoating and facilitating cell entry. Sialic acid-dependent cell entry of human enterovirus D68.,Liu Y, Sheng J, Baggen J, Meng G, Xiao C, Thibaut HJ, van Kuppeveld FJ, Rossmann MG Nat Commun. 2015 Nov 13;6:8865. doi: 10.1038/ncomms9865. PMID:26563423[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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