View source for 4yya


==The structure of hemagglutinin from a H6N1 influenza virus (A/Taiwan/2/2013) in complex with avian receptor analog 3'SLNLN==
<StructureSection load='4yya' size='340' side='right'caption='[[4yya]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yya]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/H6N1_subtype H6N1 subtype]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YYA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YYA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.595&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></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=4yya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yya OCA], [https://pdbe.org/4yya PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yya RCSB], [https://www.ebi.ac.uk/pdbsum/4yya PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yya ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0J9X268_9INFA A0A0J9X268_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 either through clathrin-dependent endocytosis or through 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.[SAAS:SAAS00842036]  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]

==See Also==
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
__TOC__
</StructureSection>
[[Category: H6N1 subtype]]
[[Category: Large Structures]]
[[Category: Bi Y]]
[[Category: Gao GF]]
[[Category: Liu J]]
[[Category: Qi J]]
[[Category: Shi Y]]
[[Category: Wang F]]
[[Category: Wang M]]
[[Category: Yan J]]
[[Category: Zhang W]]