6odf: Difference between revisions
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<StructureSection load='6odf' size='340' side='right'caption='[[6odf]], [[Resolution|resolution]] 5.80Å' scene=''> | <StructureSection load='6odf' size='340' side='right'caption='[[6odf]], [[Resolution|resolution]] 5.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6odf]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ODF OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[6odf]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Eeev Eeev]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ODF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ODF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M7J:heparin'>M7J</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M7J:heparin'>M7J</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Togavirin Togavirin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.90 3.4.21.90] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Togavirin Togavirin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.90 3.4.21.90] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6odf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6odf OCA], [http://pdbe.org/6odf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6odf RCSB], [http://www.ebi.ac.uk/pdbsum/6odf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6odf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Eastern equine encephalitis virus (EEEV), a mosquito-borne icosahedral alphavirus found mainly in North America, causes human and equine neurotropic infections. EEEV neurovirulence is influenced by the interaction of the viral envelope protein E2 with heparan sulfate (HS) proteoglycans from the host's plasma membrane during virus entry. Here, we present a 5.8-A cryoelectron microscopy (cryo-EM) structure of EEEV complexed with the HS analog heparin. "Peripheral" HS binding sites were found to be associated with the base of each of the E2 glycoproteins that form the 60 quasi-threefold spikes (q3) and the 20 sites associated with the icosahedral threefold axes (i3). In addition, there is one HS site at the vertex of each q3 and i3 spike (the "axial" sites). Both the axial and peripheral sites are surrounded by basic residues, suggesting an electrostatic mechanism for HS binding. These residues are highly conserved among EEEV strains, and therefore a change in these residues might be linked to EEEV neurovirulence. | |||
Cryo-EM structure of eastern equine encephalitis virus in complex with heparan sulfate analogues.,Chen CL, Hasan SS, Klose T, Sun Y, Buda G, Sun C, Klimstra WB, Rossmann MG Proc Natl Acad Sci U S A. 2020 Apr 3. pii: 1910670117. doi:, 10.1073/pnas.1910670117. PMID:32245806<ref>PMID:32245806</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6odf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Eeev]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Togavirin]] | [[Category: Togavirin]] | ||
[[Category: Chen, C L]] | [[Category: Chen, C L]] | ||
[[Category: Rossmann, M G]] | [[Category: Rossmann, M G]] | ||
[[Category: Virus]] | [[Category: Virus]] | ||
Revision as of 09:03, 22 April 2020
EEEV glycoproteins bound with heparan sulfateEEEV glycoproteins bound with heparan sulfate
Structural highlights
Publication Abstract from PubMedEastern equine encephalitis virus (EEEV), a mosquito-borne icosahedral alphavirus found mainly in North America, causes human and equine neurotropic infections. EEEV neurovirulence is influenced by the interaction of the viral envelope protein E2 with heparan sulfate (HS) proteoglycans from the host's plasma membrane during virus entry. Here, we present a 5.8-A cryoelectron microscopy (cryo-EM) structure of EEEV complexed with the HS analog heparin. "Peripheral" HS binding sites were found to be associated with the base of each of the E2 glycoproteins that form the 60 quasi-threefold spikes (q3) and the 20 sites associated with the icosahedral threefold axes (i3). In addition, there is one HS site at the vertex of each q3 and i3 spike (the "axial" sites). Both the axial and peripheral sites are surrounded by basic residues, suggesting an electrostatic mechanism for HS binding. These residues are highly conserved among EEEV strains, and therefore a change in these residues might be linked to EEEV neurovirulence. Cryo-EM structure of eastern equine encephalitis virus in complex with heparan sulfate analogues.,Chen CL, Hasan SS, Klose T, Sun Y, Buda G, Sun C, Klimstra WB, Rossmann MG Proc Natl Acad Sci U S A. 2020 Apr 3. pii: 1910670117. doi:, 10.1073/pnas.1910670117. PMID:32245806[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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