4we7

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==Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins==
==Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins==
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<StructureSection load='4we7' size='340' side='right' caption='[[4we7]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='4we7' size='340' side='right'caption='[[4we7]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4we7]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WE7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WE7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4we7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Alberta/026/2012(H3N2)) Influenza A virus (A/Alberta/026/2012(H3N2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WE7 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]] 2.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4we4|4we4]], [[4we5|4we5]], [[4we6|4we6]], [[4we8|4we8]], [[4we9|4we9]], [[4wea|4wea]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4we7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4we7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4we7 RCSB], [http://www.ebi.ac.uk/pdbsum/4we7 PDBsum]</span></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=4we7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4we7 OCA], [https://pdbe.org/4we7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4we7 RCSB], [https://www.ebi.ac.uk/pdbsum/4we7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4we7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/U3N7S5_9INFA U3N7S5_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/U3N7S5_9INFA U3N7S5_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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<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>
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</div>
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<div class="pdbe-citations 4we7" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Carney, P J]]
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[[Category: Large Structures]]
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[[Category: Chang, J C]]
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[[Category: Carney PJ]]
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[[Category: Guo, Z]]
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[[Category: Chang JC]]
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[[Category: Stevens, J]]
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[[Category: Guo Z]]
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[[Category: Villanueva, J M]]
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[[Category: Stevens J]]
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[[Category: Yang, H]]
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[[Category: Villanueva JM]]
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[[Category: H3n2]]
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[[Category: Yang H]]
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[[Category: Ha1]]
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[[Category: Hemagglutinin]]
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[[Category: Influenza virus]]
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Current revision

Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins

PDB ID 4we7

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