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| | <StructureSection load='4kw1' size='340' side='right'caption='[[4kw1]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='4kw1' size='340' side='right'caption='[[4kw1]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kw1]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/reassortant/idcdc_rg29(egypt/n03072/2010_x_puerto_rico/8/1934)(h5n1)) Influenza a virus (a/reassortant/idcdc_rg29(egypt/n03072/2010 x puerto rico/8/1934)(h5n1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KW1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KW1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kw1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/reassortant/IDCDC_RG29(Egypt/N03072/2010_x_Puerto_Rico/8/1934)(H5N1)) Influenza A virus (A/reassortant/IDCDC_RG29(Egypt/N03072/2010 x Puerto Rico/8/1934)(H5N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KW1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kth|4kth]], [[4kwm|4kwm]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1071165 Influenza A virus (A/reassortant/IDCDC_RG29(Egypt/N03072/2010 x Puerto Rico/8/1934)(H5N1))])</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=4kw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kw1 OCA], [https://pdbe.org/4kw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kw1 RCSB], [https://www.ebi.ac.uk/pdbsum/4kw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kw1 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=4kw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kw1 OCA], [http://pdbe.org/4kw1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kw1 RCSB], [http://www.ebi.ac.uk/pdbsum/4kw1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kw1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/G1JUF7_9INFA G1JUF7_9INFA]] 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][SAAS:SAAS013829_004_327643] | + | [https://www.uniprot.org/uniprot/G1JUF7_9INFA G1JUF7_9INFA] 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][SAAS:SAAS013829_004_327643] |
| | <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/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Carney, P J]] | + | [[Category: Carney PJ]] |
| - | [[Category: Chang, J C]] | + | [[Category: Chang JC]] |
| - | [[Category: Shore, D A]] | + | [[Category: Shore DA]] |
| - | [[Category: Stevens, J]] | + | [[Category: Stevens J]] |
| - | [[Category: Yang, H]] | + | [[Category: Yang H]] |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
G1JUF7_9INFA 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][SAAS:SAAS013829_004_327643]
Publication Abstract from PubMed
Antigenic variation among circulating H5N1 highly pathogenic avian influenza A viruses mandates the continuous production of strain-specific pre-pandemic vaccine candidates and represents a significant challenge for pandemic preparedness. Here we assessed the structural, antigenic and receptor-binding properties of three H5N1 HPAI virus hemagglutinins, which were recently selected by the WHO as vaccine candidates [A/Egypt/N03072/2010 (Egypt10, clade 2.2.1), A/Hubei/1/2010 (Hubei10, clade 2.3.2.1) and A/Anhui/1/2005 (Anhui05, clade 2.3.4)]. These analyses revealed that antigenic diversity among these three isolates was restricted to changes in the size and charge of amino acid side chains at a handful of positions, spatially equivalent to the antigenic sites identified in H1 subtype viruses circulating among humans. All three of the H5N1 viruses analyzed in this study were responsible for fatal human infections, with the most recently-isolated strains, Hubei10 and Egypt10, containing multiple residues in the receptor-binding site of the HA, which were suspected to enhance mammalian transmission. However, glycan-binding analyses demonstrated a lack of binding to human alpha2-6-linked sialic acid receptor analogs for all three HAs, reinforcing the notion that receptor-binding specificity contributes only partially to transmissibility and pathogenesis of HPAI viruses and suggesting that changes in host specificity must be interpreted in the context of the host and environmental factors, as well as the virus as a whole. Together, our data reveal structural linkages with phylogenetic and antigenic analyses of recently emerged H5N1 virus clades and should assist in interpreting the significance of future changes in antigenic and receptor-binding properties.
Structural and Antigenic Variation among Diverse Clade 2 H5N1 Viruses.,Shore DA, Yang H, Balish AL, Shepard SS, Carney PJ, Chang JC, Davis CT, Donis RO, Villanueva JM, Klimov AI, Stevens J PLoS One. 2013 Sep 27;8(9):e75209. doi: 10.1371/journal.pone.0075209. PMID:24086467[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shore DA, Yang H, Balish AL, Shepard SS, Carney PJ, Chang JC, Davis CT, Donis RO, Villanueva JM, Klimov AI, Stevens J. Structural and Antigenic Variation among Diverse Clade 2 H5N1 Viruses. PLoS One. 2013 Sep 27;8(9):e75209. doi: 10.1371/journal.pone.0075209. PMID:24086467 doi:http://dx.doi.org/10.1371/journal.pone.0075209
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