4fqm

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==Structure of B/Brisbane/60/2008 Influenza Hemagglutinin==
==Structure of B/Brisbane/60/2008 Influenza Hemagglutinin==
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<StructureSection load='4fqm' size='340' side='right' caption='[[4fqm]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
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<StructureSection load='4fqm' size='340' side='right'caption='[[4fqm]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fqm]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_b_virus_(b/brisbane/60/2008) Influenza b virus (b/brisbane/60/2008)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FQM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fqm]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_B_virus_(B/Brisbane/60/2008) Influenza B virus (B/Brisbane/60/2008)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FQM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fnk|4fnk]], [[4fqh|4fqh]], [[4fqi|4fqi]], [[4fqj|4fqj]], [[4fqk|4fqk]], [[4fql|4fql]], [[4fqv|4fqv]], [[4fqy|4fqy]]</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=4fqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqm OCA], [https://pdbe.org/4fqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fqm RCSB], [https://www.ebi.ac.uk/pdbsum/4fqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fqm ProSAT]</span></td></tr>
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<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=604436 Influenza B virus (B/Brisbane/60/2008)])</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=4fqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqm OCA], [http://pdbe.org/4fqm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fqm RCSB], [http://www.ebi.ac.uk/pdbsum/4fqm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fqm ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/C0LT38_9INFB C0LT38_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/C0LT38_9INFB C0LT38_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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==See Also==
==See Also==
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*[[Hemagglutinin|Hemagglutinin]]
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Dreyfus, C]]
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[[Category: Large Structures]]
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[[Category: Laursen, N S]]
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[[Category: Dreyfus C]]
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[[Category: Wilson, I A]]
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[[Category: Laursen NS]]
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[[Category: Hemagglutinin]]
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[[Category: Wilson IA]]
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[[Category: Influenza b virus]]
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[[Category: Viral protein]]
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Revision as of 20:06, 19 October 2022

Structure of B/Brisbane/60/2008 Influenza Hemagglutinin

PDB ID 4fqm

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