5xl9
From Proteopedia
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==The structure of hemagglutinin G228S mutant from an avian-origin H4N6 influenza virus in complex with avian receptor analog LSTa== | ==The structure of hemagglutinin G228S mutant from an avian-origin H4N6 influenza virus in complex with avian receptor analog LSTa== | ||
| - | <StructureSection load='5xl9' size='340' side='right' caption='[[5xl9]], [[Resolution|resolution]] 2.39Å' scene=''> | + | <StructureSection load='5xl9' size='340' side='right'caption='[[5xl9]], [[Resolution|resolution]] 2.39Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5xl9]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XL9 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5xl9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/duck/Czechoslovakia/1956(H4N6)) Influenza A virus (A/duck/Czechoslovakia/1956(H4N6))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XL9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XL9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.39Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></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=5xl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xl9 OCA], [https://pdbe.org/5xl9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xl9 RCSB], [https://www.ebi.ac.uk/pdbsum/5xl9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xl9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/HEMA_I56A1 HEMA_I56A1] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[HAMAP-Rule:MF_04072] |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5xl9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5xl9" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Gao FG]] |
| - | [[Category: | + | [[Category: Qi J]] |
| - | [[Category: | + | [[Category: Song H]] |
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| - | + | ||
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Current revision
The structure of hemagglutinin G228S mutant from an avian-origin H4N6 influenza virus in complex with avian receptor analog LSTa
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Categories: Large Structures | Gao FG | Qi J | Song H
