4we5: Difference between revisions
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==The crystal structure of hemagglutinin from A/Port Chalmers/1/1973 influenza virus== | ==The crystal structure of hemagglutinin from A/Port Chalmers/1/1973 influenza virus== | ||
<StructureSection load='4we5' size='340' side='right' caption='[[4we5]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='4we5' size='340' side='right'caption='[[4we5]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4we5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WE5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4we5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/I73a5 I73a5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WE5 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='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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4we4|4we4]], [[4we6|4we6]], [[4we7|4we7]], [[4we8|4we8]], [[4we9|4we9]], [[4wea|4wea]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4we4|4we4]], [[4we6|4we6]], [[4we7|4we7]], [[4we8|4we8]], [[4we9|4we9]], [[4wea|4wea]]</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=385624 I73A5])</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=4we5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4we5 OCA], [http://pdbe.org/4we5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4we5 RCSB], [http://www.ebi.ac.uk/pdbsum/4we5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4we5 ProSAT]</span></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=4we5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4we5 OCA], [http://pdbe.org/4we5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4we5 RCSB], [http://www.ebi.ac.uk/pdbsum/4we5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4we5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: I73a5]] | |||
[[Category: Large Structures]] | |||
[[Category: Carney, P J]] | [[Category: Carney, P J]] | ||
[[Category: Chang, J C]] | [[Category: Chang, J C]] | ||
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[[Category: Hemagglutinin]] | [[Category: Hemagglutinin]] | ||
[[Category: Influenza virus]] | [[Category: Influenza virus]] | ||
[[Category: Viral protein]] | |||
Revision as of 11:58, 23 May 2019
The crystal structure of hemagglutinin from A/Port Chalmers/1/1973 influenza virusThe crystal structure of hemagglutinin from A/Port Chalmers/1/1973 influenza virus
Structural highlights
Function[HEMA_I73A5] 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 PubMedA(H3N2) influenza viruses have circulated in humans since 1968, and antigenic drift of the hemagglutinin (HA) protein continues to be a driving force that allows the virus to escape the human immune response. Since the major antigenic sites of the HA overlap into the receptor binding site (RBS) of the molecule, the virus constantly struggles to effectively adapt to host immune responses, without compromising its functionality. Here, we have structurally assessed the evolution of the A(H3N2) virus HA RBS, using an established recombinant expression system. Glycan binding specificities of nineteen A(H3N2) influenza virus HAs, each a component of the seasonal influenza vaccine between 1968 and 2012, were analyzed. Results suggest that while its receptor-binding site has evolved from one that can bind a broad range of human receptor analogs to one with a more restricted binding profile for longer glycans, the virus continues to circulate and transmit efficiently among humans. Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins.,Yang H, Carney PJ, Chang JC, Guo Z, Villanueva JM, Stevens J Virology. 2015 Jan 21;477C:18-31. doi: 10.1016/j.virol.2014.12.024. PMID:25617824[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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