1ru7: Difference between revisions
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<StructureSection load='1ru7' size='340' side='right'caption='[[1ru7]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1ru7' size='340' side='right'caption='[[1ru7]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ru7]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ru7]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_a_virus_(a/puerto_rico/8/34(h1n1)) Influenza a virus (a/puerto rico/8/34(h1n1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RU7 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ruy|1ruy]], [[1ruz|1ruz]], [[1rv0|1rv0]], [[1rvt|1rvt]], [[1rvx|1rvx]], [[1rvz|1rvz]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ruy|1ruy]], [[1ruz|1ruz]], [[1rv0|1rv0]], [[1rvt|1rvt]], [[1rvx|1rvx]], [[1rvz|1rvz]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ru7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ru7 OCA], [https://pdbe.org/1ru7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ru7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ru7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ru7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/Q82766_9INFA Q82766_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:SAAS013827_004_327643] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |