9mti
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of porcine Fab 15-1 in complex with influenza H3N8 A/Mallard/Alberta/362/2017 hemagglutinin== | |
| - | + | <StructureSection load='9mti' size='340' side='right'caption='[[9mti]], [[Resolution|resolution]] 2.98Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9mti]] is a 9 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=9MTI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MTI 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]] 2.98Å</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=9mti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9mti OCA], [https://pdbe.org/9mti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9mti RCSB], [https://www.ebi.ac.uk/pdbsum/9mti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9mti ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [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] | ||
| + | __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 15-1 in complex with influenza H3N8 A/Mallard/Alberta/362/2017 hemagglutinin
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