5dup

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==Influenza A virus H5 hemagglutinin globular head in complex with antibody AVFluIgG03==
==Influenza A virus H5 hemagglutinin globular head in complex with antibody AVFluIgG03==
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<StructureSection load='5dup' size='340' side='right' caption='[[5dup]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
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<StructureSection load='5dup' size='340' side='right'caption='[[5dup]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5dup]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DUP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5dup]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Anhui/1/2005(H5N1)) Influenza A virus (A/Anhui/1/2005(H5N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DUP FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dum|5dum]], [[5dur|5dur]], [[5dut|5dut]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.052&#8491;</td></tr>
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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=5dup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dup OCA], [http://pdbe.org/5dup PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dup RCSB], [http://www.ebi.ac.uk/pdbsum/5dup PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5dup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dup OCA], [https://pdbe.org/5dup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dup RCSB], [https://www.ebi.ac.uk/pdbsum/5dup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dup ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/Q1WDM0_9INFA Q1WDM0_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:SAAS013829_004_327643]
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[https://www.uniprot.org/uniprot/Q1WDM0_9INFA Q1WDM0_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:SAAS013829_004_327643]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5dup" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5dup" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Sun, J]]
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[[Category: Homo sapiens]]
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[[Category: Wang, G]]
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[[Category: Large Structures]]
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[[Category: Wang, X]]
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[[Category: Sun J]]
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[[Category: Zhang, L]]
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[[Category: Wang G]]
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[[Category: Zhou, P]]
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[[Category: Wang X]]
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[[Category: Zuo, T]]
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[[Category: Zhang L]]
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[[Category: Antibody]]
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[[Category: Zhou P]]
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[[Category: Complex]]
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[[Category: Zuo T]]
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[[Category: Immune system]]
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[[Category: Influenza virus]]
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[[Category: Neutralize]]
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Current revision

Influenza A virus H5 hemagglutinin globular head in complex with antibody AVFluIgG03

PDB ID 5dup

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