4nkj

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==Structure of influenza B virus hemagglutinin at membrane fusion pH==
==Structure of influenza B virus hemagglutinin at membrane fusion pH==
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<StructureSection load='4nkj' size='340' side='right' caption='[[4nkj]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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<StructureSection load='4nkj' size='340' side='right'caption='[[4nkj]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4nkj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_b_virus_(b/texas/3394/2013) Influenza b virus (b/texas/3394/2013)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NKJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NKJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4nkj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_B_virus_(B/Texas/3394/2013) Influenza B virus (B/Texas/3394/2013)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NKJ FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1354485 Influenza B virus (B/Texas/3394/2013)])</td></tr>
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</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=4nkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nkj OCA], [https://pdbe.org/4nkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nkj RCSB], [https://www.ebi.ac.uk/pdbsum/4nkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nkj ProSAT]</span></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=4nkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nkj OCA], [http://pdbe.org/4nkj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nkj RCSB], [http://www.ebi.ac.uk/pdbsum/4nkj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nkj ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/S5DRP1_9INFB S5DRP1_9INFB]] 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]
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[https://www.uniprot.org/uniprot/S5DRP1_9INFB S5DRP1_9INFB] 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]
<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 4nkj" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4nkj" 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: Chen, X]]
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[[Category: Large Structures]]
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[[Category: Ni, F]]
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[[Category: Chen X]]
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[[Category: Shen, J]]
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[[Category: Ni F]]
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[[Category: Wang, Q]]
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[[Category: Shen J]]
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[[Category: Ha]]
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[[Category: Wang Q]]
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[[Category: Viral protein]]
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Revision as of 08:32, 11 January 2023

Structure of influenza B virus hemagglutinin at membrane fusion pH

PDB ID 4nkj

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