4n61

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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=4n61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n61 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n61 RCSB], [http://www.ebi.ac.uk/pdbsum/4n61 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=4n61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n61 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n61 RCSB], [http://www.ebi.ac.uk/pdbsum/4n61 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/R4NN21_9INFA R4NN21_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]
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 21:35, 25 December 2014

Crystal structure of hemagglutinin from an H7N9 influenza virus in complex with LSTa, extended soaking

4n61, resolution 2.60Å

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