5e66: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='5e66' size='340' side='right' caption='[[5e66]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='5e66' size='340' side='right' caption='[[5e66]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5e66]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E66 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5e66]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_c_virus_(c/swine/oklahoma/1334/2011) Influenza c virus (c/swine/oklahoma/1334/2011)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E66 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5KQ:(6R)-5-(ACETYLAMINO)-6-[(1S,2S)-3-(ACETYLAMINO)-1,2-DIHYDROXYPROPYL]-3,5-DIDEOXY-BETA-L-THREO-HEX-2-ULOPYRANOSONIC+ACID'>5KQ</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5KQ:(6R)-5-(ACETYLAMINO)-6-[(1S,2S)-3-(ACETYLAMINO)-1,2-DIHYDROXYPROPYL]-3,5-DIDEOXY-BETA-L-THREO-HEX-2-ULOPYRANOSONIC+ACID'>5KQ</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e62|5e62]], [[5e65|5e65]], [[5e64|5e64]], [[5e5w|5e5w]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e62|5e62]], [[5e65|5e65]], [[5e64|5e64]], [[5e5w|5e5w]]</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=5e66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e66 OCA], [http://pdbe.org/5e66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e66 RCSB], [http://www.ebi.ac.uk/pdbsum/5e66 PDBsum]</span></td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HEF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1173138 Influenza C virus (C/swine/Oklahoma/1334/2011)])</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=5e66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e66 OCA], [http://pdbe.org/5e66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e66 RCSB], [http://www.ebi.ac.uk/pdbsum/5e66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e66 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Influenza viruses cause seasonal flu each year and pandemics or epidemic sporadically, posing a major threat to public health. Recently, a new influenza D virus (IDV) was isolated from pigs and cattle. Here, we reveal that the IDV utilizes 9-O-acetylated sialic acids as its receptor for virus entry. Then, we determined the crystal structures of hemagglutinin-esterase-fusion glycoprotein (HEF) of IDV both in its free form and in complex with the receptor and enzymatic substrate analogs. The IDV HEF shows an extremely similar structural fold as the human-infecting influenza C virus (ICV) HEF. However, IDV HEF has an open receptor-binding cavity to accommodate diverse extended glycan moieties. This structural difference provides an explanation for the phenomenon that the IDV has a broad cell tropism. As IDV HEF is structurally and functionally similar to ICV HEF, our findings highlight the potential threat of the virus to public health. | |||
An Open Receptor-Binding Cavity of Hemagglutinin-Esterase-Fusion Glycoprotein from Newly-Identified Influenza D Virus: Basis for Its Broad Cell Tropism.,Song H, Qi J, Khedri Z, Diaz S, Yu H, Chen X, Varki A, Shi Y, Gao GF PLoS Pathog. 2016 Jan 27;12(1):e1005411. doi: 10.1371/journal.ppat.1005411., eCollection 2016 Jan. PMID:26816272<ref>PMID:26816272</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 5e66" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5e66" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Hemagglutinin-esterase|Hemagglutinin-esterase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:20, 5 September 2018
The complex structure of Hemagglutinin-esterase-fusion mutant protein from the influenza D virus with receptor analog 9-N-Ac-SiaThe complex structure of Hemagglutinin-esterase-fusion mutant protein from the influenza D virus with receptor analog 9-N-Ac-Sia
Structural highlights
Publication Abstract from PubMedInfluenza viruses cause seasonal flu each year and pandemics or epidemic sporadically, posing a major threat to public health. Recently, a new influenza D virus (IDV) was isolated from pigs and cattle. Here, we reveal that the IDV utilizes 9-O-acetylated sialic acids as its receptor for virus entry. Then, we determined the crystal structures of hemagglutinin-esterase-fusion glycoprotein (HEF) of IDV both in its free form and in complex with the receptor and enzymatic substrate analogs. The IDV HEF shows an extremely similar structural fold as the human-infecting influenza C virus (ICV) HEF. However, IDV HEF has an open receptor-binding cavity to accommodate diverse extended glycan moieties. This structural difference provides an explanation for the phenomenon that the IDV has a broad cell tropism. As IDV HEF is structurally and functionally similar to ICV HEF, our findings highlight the potential threat of the virus to public health. An Open Receptor-Binding Cavity of Hemagglutinin-Esterase-Fusion Glycoprotein from Newly-Identified Influenza D Virus: Basis for Its Broad Cell Tropism.,Song H, Qi J, Khedri Z, Diaz S, Yu H, Chen X, Varki A, Shi Y, Gao GF PLoS Pathog. 2016 Jan 27;12(1):e1005411. doi: 10.1371/journal.ppat.1005411., eCollection 2016 Jan. PMID:26816272[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||