4f3z

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==Crystal structure of a swine H1N2 influenza virus hemagglutinin==
==Crystal structure of a swine H1N2 influenza virus hemagglutinin==
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<StructureSection load='4f3z' size='340' side='right' caption='[[4f3z]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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<StructureSection load='4f3z' size='340' side='right'caption='[[4f3z]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4f3z]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F3Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F3Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4f3z]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Swine/Indiana/P12439/00_(H1N2)) Influenza A virus (A/Swine/Indiana/P12439/00 (H1N2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F3Z FirstGlance]. <br>
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</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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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<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=4f3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f3z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f3z RCSB], [http://www.ebi.ac.uk/pdbsum/4f3z PDBsum]</span></td></tr>
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<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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f3z OCA], [https://pdbe.org/4f3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f3z RCSB], [https://www.ebi.ac.uk/pdbsum/4f3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f3z ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/Q8QT89_9INFA Q8QT89_9INFA]] 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.[RuleBase:RU003324][SAAS:SAAS00145386]
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[https://www.uniprot.org/uniprot/Q8QT89_9INFA Q8QT89_9INFA] 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.[RuleBase:RU003324][SAAS:SAAS00145386]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4f3z" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Hemagglutinin|Hemagglutinin]]
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Influenza a virus]]
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[[Category: Large Structures]]
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[[Category: Wilson, I A]]
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[[Category: Wilson IA]]
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[[Category: Xu, R]]
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[[Category: Xu R]]
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[[Category: Sialic acid]]
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[[Category: Viral envelope protein]]
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[[Category: Viral protein]]
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[[Category: Viral receptor binding and fusion protein]]
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Current revision

Crystal structure of a swine H1N2 influenza virus hemagglutinin

PDB ID 4f3z

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