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4fqj

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fqj RCSB], [http://www.ebi.ac.uk/pdbsum/4fqj PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fqj RCSB], [http://www.ebi.ac.uk/pdbsum/4fqj PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/I0B7N4_9INFB I0B7N4_9INFB]] 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.[RuleBase:RU003324]
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 16:38, 25 December 2014

Influenza B/Florida/4/2006 hemagglutinin Fab CR8071 complex

4fqj, resolution 2.50Å

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