4lvh: Difference between revisions
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<StructureSection load='4lvh' size='340' side='right'caption='[[4lvh]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='4lvh' size='340' side='right'caption='[[4lvh]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lvh]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4lvh]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Korea/01/2009(H1N1)) Influenza A virus (A/Korea/01/2009(H1N1))] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LVH FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=4lvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lvh OCA], [https://pdbe.org/4lvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lvh RCSB], [https://www.ebi.ac.uk/pdbsum/4lvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lvh ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/C5MQE6_9INFA C5MQE6_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 (By similarity).[RuleBase:RU003324][SAAS:SAAS008980_004_327643] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Cho | [[Category: Cho KJ]] | ||
[[Category: Kim | [[Category: Kim KH]] | ||
[[Category: Kim | [[Category: Kim S]] | ||
[[Category: Lee | [[Category: Lee J-H]] | ||
[[Category: Seok | [[Category: Seok JH]] | ||