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==Structure of hemagglutinin with F95Y mutation of influenza virus B/Lee/40==
==Structure of hemagglutinin with F95Y mutation of influenza virus B/Lee/40==
<StructureSection load='4nrl' size='340' side='right' caption='[[4nrl]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
<StructureSection load='4nrl' size='340' side='right'caption='[[4nrl]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4nrl]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Inble Inble]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NRL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NRL FirstGlance]. <br>
<table><tr><td colspan='2'>[[4nrl]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_B_virus_(B/Lee/1940) Influenza B virus (B/Lee/1940)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NRL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</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]] 2.72&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4nrj|4nrj]], [[4nrk|4nrk]]</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=4nrl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrl OCA], [https://pdbe.org/4nrl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nrl RCSB], [https://www.ebi.ac.uk/pdbsum/4nrl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nrl ProSAT]</span></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=107412 INBLE])</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=4nrl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrl OCA], [http://pdbe.org/4nrl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nrl RCSB], [http://www.ebi.ac.uk/pdbsum/4nrl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nrl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HEMA_INBLE HEMA_INBLE]] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. 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 induce an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.  
[https://www.uniprot.org/uniprot/HEMA_INBLE HEMA_INBLE] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. 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 induce an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.
<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==
*[[Hemagglutinin|Hemagglutinin]]
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Inble]]
[[Category: Large Structures]]
[[Category: Kondrashkina, E]]
[[Category: Kondrashkina E]]
[[Category: Mbawuike, I N]]
[[Category: Mbawuike IN]]
[[Category: Ni, F]]
[[Category: Ni F]]
[[Category: Wang, Q]]
[[Category: Wang Q]]
[[Category: Ha]]
[[Category: Viral protein]]
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