9mtf
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of porcine Fab 14-1 in complex with influenza H1N1 A/Solomon Island/3/2006 hemagglutinin== | |
| - | + | <StructureSection load='9mtf' size='340' side='right'caption='[[9mtf]], [[Resolution|resolution]] 2.61Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9mtf]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Solomon_Islands/3/2006(H1N1)) Influenza A virus (A/Solomon Islands/3/2006(H1N1))] 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=9MTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MTF 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]] 2.61Å</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=9mtf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9mtf OCA], [https://pdbe.org/9mtf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9mtf RCSB], [https://www.ebi.ac.uk/pdbsum/9mtf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9mtf ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0G2RTI0_9INFA A0A0G2RTI0_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.[ARBA:ARBA00059860][RuleBase:RU003324] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Sus scrofa]] | ||
| + | [[Category: Lv H]] | ||
| + | [[Category: Pholcharee T]] | ||
| + | [[Category: Wu NC]] | ||
Current revision
Structure of porcine Fab 14-1 in complex with influenza H1N1 A/Solomon Island/3/2006 hemagglutinin
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