9mtl
From Proteopedia
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(New page: '''Unreleased structure''' The entry 9mtl is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of porcine Fab 24-1G23 in complex with influenza H1N1 A/Hawaii/70/2019 hemagglutinin== | |
| - | + | <StructureSection load='9mtl' size='340' side='right'caption='[[9mtl]], [[Resolution|resolution]] 2.41Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9mtl]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus Influenza A virus] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9MTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MTL FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.41Å</td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9mtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9mtl OCA], [https://pdbe.org/9mtl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9mtl RCSB], [https://www.ebi.ac.uk/pdbsum/9mtl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9mtl ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A7U0YFD5_9INFA A0A7U0YFD5_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] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Influenza A virus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Sus scrofa]] | ||
| + | [[Category: Lv H]] | ||
| + | [[Category: Pholcharee T]] | ||
| + | [[Category: Wu NC]] | ||
Current revision
Structure of porcine Fab 24-1G23 in complex with influenza H1N1 A/Hawaii/70/2019 hemagglutinin
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