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==Crystal structure of influenza A virus H5 hemagglutinin globular head in complex with the Fab of antibody FLD21.140==
==Crystal structure of influenza A virus H5 hemagglutinin globular head in complex with the Fab of antibody FLD21.140==
<StructureSection load='6a67' size='340' side='right' caption='[[6a67]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
<StructureSection load='6a67' size='340' side='right'caption='[[6a67]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6a67]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/thailand/1(kan-1)/2004(h5n1)) Influenza a virus (a/thailand/1(kan-1)/2004(h5n1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A67 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6a67]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Thailand/1(KAN-1)/2004(H5N1)) Influenza A virus (A/Thailand/1(KAN-1)/2004(H5N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A67 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33&#8491;</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=6a67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a67 OCA], [http://pdbe.org/6a67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a67 RCSB], [http://www.ebi.ac.uk/pdbsum/6a67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a67 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6a67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a67 OCA], [https://pdbe.org/6a67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a67 RCSB], [https://www.ebi.ac.uk/pdbsum/6a67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a67 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/Q6Q794_9INFA Q6Q794_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:SAAS01039674]  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]  
[https://www.uniprot.org/uniprot/Q6Q794_9INFA Q6Q794_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:SAAS01039674]  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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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6a67" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6a67" style="background-color:#fffaf0;"></div>
==See Also==
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Sun, J]]
[[Category: Large Structures]]
[[Category: Wang, P]]
[[Category: Sun J]]
[[Category: Wang, X]]
[[Category: Wang P]]
[[Category: Zhang, L]]
[[Category: Wang X]]
[[Category: Zuo, Y]]
[[Category: Zhang L]]
[[Category: H5n1]]
[[Category: Zuo Y]]
[[Category: Immune system]]
[[Category: Influenza virus]]
[[Category: Neutralizing antibody]]
[[Category: Receptor binding site]]

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