9n4f

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Current revision (07:29, 8 October 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9n4f is ON HOLD until Paper Publication
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==Structure of 240-14-IgA_2F02 Fab in complex with influenza H3N8 A/Mallard/Alberta/362/2017 Hemagglutinin==
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<StructureSection load='9n4f' size='340' side='right'caption='[[9n4f]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
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Authors: Gopal, A.B., Wu, N.C., Lv, H., Pholcharee, T.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9n4f]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://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=9N4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9N4F FirstGlance]. <br>
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Description: Structure of 240-14-IgA_2F02 Fab in complex with influenza H3N8 A/Mallard/Alberta/362/2017 Hemagglutinin
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.71&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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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=9n4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9n4f OCA], [https://pdbe.org/9n4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9n4f RCSB], [https://www.ebi.ac.uk/pdbsum/9n4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9n4f ProSAT]</span></td></tr>
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[[Category: Gopal, A.B]]
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</table>
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[[Category: Pholcharee, T]]
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== Function ==
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[[Category: Wu, N.C]]
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[https://www.uniprot.org/uniprot/A0A2Z4WF96_9INFA A0A2Z4WF96_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 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] 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.[ARBA:ARBA00059860][RuleBase:RU003324]
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[[Category: Lv, H]]
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Influenza A virus]]
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[[Category: Large Structures]]
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[[Category: Gopal AB]]
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[[Category: Lv H]]
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[[Category: Pholcharee T]]
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[[Category: Wu NC]]

Current revision

Structure of 240-14-IgA_2F02 Fab in complex with influenza H3N8 A/Mallard/Alberta/362/2017 Hemagglutinin

PDB ID 9n4f

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