5n11: Difference between revisions
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==Crystal structure of Human beta1-coronavirus OC43 NL/A/2005 Hemagglutinin-Esterase== | ==Crystal structure of Human beta1-coronavirus OC43 NL/A/2005 Hemagglutinin-Esterase== | ||
<StructureSection load='5n11' size='340' side='right' caption='[[5n11]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='5n11' size='340' side='right'caption='[[5n11]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5n11]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N11 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5n11]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvhoc Cvhoc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N11 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5N11 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand= | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31631 CVHOC])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sialate_O-acetylesterase Sialate O-acetylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.53 3.1.1.53] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sialate_O-acetylesterase Sialate O-acetylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.53 3.1.1.53] </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=5n11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n11 OCA], [http://pdbe.org/5n11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n11 RCSB], [http://www.ebi.ac.uk/pdbsum/5n11 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n11 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5n11" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5n11" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Hemagglutinin-esterase 3D structures|Hemagglutinin-esterase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cvhoc]] | |||
[[Category: Large Structures]] | |||
[[Category: Sialate O-acetylesterase]] | [[Category: Sialate O-acetylesterase]] | ||
[[Category: Bakkers, M J.G]] | [[Category: Bakkers, M J.G]] | ||
Revision as of 14:55, 26 August 2020
Structural highlights
Function[Q4VID6_CVHOC] May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Seems to be a 'luxury' protein that is not absolutely necessary for virus infection in culture.[RuleBase:RU361278] Publication Abstract from PubMedHuman beta1-coronavirus (beta1CoV) OC43 emerged relatively recently through a single zoonotic introduction. Like related animal beta1CoVs, OC43 uses 9-O-acetylated sialic acid as receptor determinant. beta1CoV receptor binding is typically controlled by attachment/fusion spike protein S and receptor-binding/receptor-destroying hemagglutinin-esterase protein HE. We show that following OC43's introduction into humans, HE-mediated receptor binding was selected against and ultimately lost through progressive accumulation of mutations in the HE lectin domain. Consequently, virion-associated receptor-destroying activity toward multivalent glycoconjugates was reduced and altered such that some clustered receptor populations are no longer cleaved. Loss of HE lectin function was also observed for another respiratory human coronavirus, HKU1. This thus appears to be an adaptation to the sialoglycome of the human respiratory tract and for replication in human airways. The findings suggest that the dynamics of virion-glycan interactions contribute to host tropism. Our observations are relevant also to other human respiratory viruses of zoonotic origin, particularly influenza A virus. Betacoronavirus Adaptation to Humans Involved Progressive Loss of Hemagglutinin-Esterase Lectin Activity.,Bakkers MJ, Lang Y, Feitsma LJ, Hulswit RJ, de Poot SA, van Vliet AL, Margine I, de Groot-Mijnes JD, van Kuppeveld FJ, Langereis MA, Huizinga EG, de Groot RJ Cell Host Microbe. 2017 Mar 8;21(3):356-366. doi: 10.1016/j.chom.2017.02.008. PMID:28279346[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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