View source for 9gsp


==Structure of uncleaved Influenza A/Victoria/2570/2019 Haemagglutinin. The 2021 Influenza A(H1N1)pdm09 egg-derived vaccine candidate.==
<StructureSection load='9gsp' size='340' side='right'caption='[[9gsp]], [[Resolution|resolution]] 3.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9gsp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/H1N1_subtype H1N1 subtype]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9GSP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9GSP 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]] 3.68&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9gsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9gsp OCA], [https://pdbe.org/9gsp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9gsp RCSB], [https://www.ebi.ac.uk/pdbsum/9gsp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9gsp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A6M4YP75_9INFA A0A6M4YP75_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: H1N1 subtype]]
[[Category: Large Structures]]
[[Category: Akbar S]]
[[Category: Anne Scott K]]
[[Category: Bhella D]]
[[Category: Dibben O]]
[[Category: Meir A]]
[[Category: Petrov F]]
[[Category: Smith T]]
[[Category: Waraich K]]