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==Crystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin HA1 Cys30, HA2 Cys47 mutant== | ==Crystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin HA1 Cys30, HA2 Cys47 mutant== | ||
<StructureSection load='4zcj' size='340' side='right' caption='[[4zcj]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4zcj' size='340' side='right'caption='[[4zcj]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4zcj]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZCJ OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4zcj]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Hong_Kong/1/1968(H3N2)) Influenza A virus (A/Hong Kong/1/1968(H3N2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZCJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZCJ FirstGlance]. <br> | ||
</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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zcj OCA], [https://pdbe.org/4zcj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zcj RCSB], [https://www.ebi.ac.uk/pdbsum/4zcj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zcj ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/HEMA_I68A4 HEMA_I68A4] 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). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 4zcj" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4zcj" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Lee PS]] | ||
[[Category: | [[Category: Wilson IA]] | ||
Latest revision as of 11:15, 27 September 2023
Crystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin HA1 Cys30, HA2 Cys47 mutantCrystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin HA1 Cys30, HA2 Cys47 mutant
Structural highlights
FunctionHEMA_I68A4 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). Publication Abstract from PubMedWe engineered a disulfide-stabilized influenza hemagglutinin (HA) trimer, termed HA3-SS, by introducing cysteine residues in the HA stem to covalently bridge the three protomers. HA3-SS has increased thermostability compared to wild-type HA and binding of head- and stem-targeted antibodies is preserved; only minor structural changes are found in the vicinity of the additional disulfide. This platform has been applied to H1 and H3 HAs and provides prospects for design of intact, stabilized influenza HA immunogens. Design and Structure of an Engineered Disulfide-Stabilized Influenza Hemagglutinin Trimer.,Lee PS, Zhu X, Yu W, Wilson IA J Virol. 2015 Apr 29. pii: JVI.00808-15. PMID:25926650[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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