1qu1: Difference between revisions
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<StructureSection load='1qu1' size='340' side='right'caption='[[1qu1]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1qu1' size='340' side='right'caption='[[1qu1]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1qu1]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1qu1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/9infa 9infa]. The April 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Hemagglutinin'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_4 10.2210/rcsb_pdb/mom_2006_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QU1 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=1qu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qu1 OCA], [https://pdbe.org/1qu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qu1 RCSB], [https://www.ebi.ac.uk/pdbsum/1qu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qu1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/HEMA_I68A0 HEMA_I68A0]] 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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == |