9mq7

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Current revision (08:22, 13 August 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9mq7 is ON HOLD until Paper Publication
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==Cryo-EM structure of hemagglutinin H5N1 in complex with Fab 326-366.26==
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<StructureSection load='9mq7' size='340' side='right'caption='[[9mq7]], [[Resolution|resolution]] 3.63&Aring;' scene=''>
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Authors: Malla, T.N., Tsybovsky, Y., Zhou, T.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9mq7]] 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=9MQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MQ7 FirstGlance]. <br>
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Description: Cryo-EM structure of hemagglutinin H5N1 in complex with Fab 326-366.26
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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]] 3.63&#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=9mq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9mq7 OCA], [https://pdbe.org/9mq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9mq7 RCSB], [https://www.ebi.ac.uk/pdbsum/9mq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9mq7 ProSAT]</span></td></tr>
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[[Category: Tsybovsky, Y]]
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</table>
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[[Category: Zhou, T]]
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== Function ==
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[[Category: Malla, T.N]]
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[https://www.uniprot.org/uniprot/A0AAX6NN08_9INFA A0AAX6NN08_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.[RuleBase:RU003324]
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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: Malla TN]]
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[[Category: Tsybovsky Y]]
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[[Category: Zhou T]]

Current revision

Cryo-EM structure of hemagglutinin H5N1 in complex with Fab 326-366.26

PDB ID 9mq7

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