9dpc

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Current revision (06:31, 19 March 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9dpc is ON HOLD until Paper Publication
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==Structure of Fab 297 in complex with influenza H1N1 A/Victoria/4897/2022 neuraminidase==
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<StructureSection load='9dpc' size='340' side='right'caption='[[9dpc]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
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Authors: Pholcharee, T., Wu, N.C.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9dpc]] is a 6 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=9DPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9DPC FirstGlance]. <br>
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Description: Structure of Fab 297 in complex with influenza H1N1 A/Victoria/4897/2022 neuraminidase
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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]] 2.65&#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=9dpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9dpc OCA], [https://pdbe.org/9dpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9dpc RCSB], [https://www.ebi.ac.uk/pdbsum/9dpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9dpc ProSAT]</span></td></tr>
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[[Category: Pholcharee, T]]
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</table>
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[[Category: Wu, N.C]]
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== Function ==
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[https://www.uniprot.org/uniprot/A0A6H1QYJ4_9INFA A0A6H1QYJ4_9INFA] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.[HAMAP-Rule:MF_04071]
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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: Pholcharee T]]
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[[Category: Wu NC]]

Current revision

Structure of Fab 297 in complex with influenza H1N1 A/Victoria/4897/2022 neuraminidase

PDB ID 9dpc

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