3lzg

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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=3lzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lzg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lzg RCSB], [http://www.ebi.ac.uk/pdbsum/3lzg 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=3lzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lzg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lzg RCSB], [http://www.ebi.ac.uk/pdbsum/3lzg PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/C3W5S1_I09A0 C3W5S1_I09A0]] 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).[SAAS:SAAS013829_004_327643][RuleBase:RU003324]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 02:49, 25 December 2014

Crystal structure of a 2009 H1N1 influenza virus hemagglutinin

3lzg, resolution 2.60Å

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