4o5n
From Proteopedia
(Difference between revisions)
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<StructureSection load='4o5n' size='340' side='right' caption='[[4o5n]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='4o5n' size='340' side='right' caption='[[4o5n]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4o5n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/singapore/h2011.447/2011(h3n2)) Influenza a virus (a/singapore/h2011.447/2011(h3n2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O5N OCA]. <br> | + | <table><tr><td colspan='2'>[[4o5n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/singapore/h2011.447/2011(h3n2)) Influenza a virus (a/singapore/h2011.447/2011(h3n2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O5N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O5N FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>< | + | </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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o58|4o58]], [[4o5i|4o5i]], [[4o5l|4o5l]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o58|4o58]], [[4o5i|4o5i]], [[4o5l|4o5l]]</td></tr> |
| - | <tr><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=1331560 Influenza A virus (A/Singapore/H2011.447/2011(H3N2))])</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=1331560 Influenza A virus (A/Singapore/H2011.447/2011(H3N2))])</td></tr> |
| - | <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=4o5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o5n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o5n RCSB], [http://www.ebi.ac.uk/pdbsum/4o5n PDBsum]</span></td></tr> |
| - | + | </table> | |
| - | <table> | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/R9U684_9INFA R9U684_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).[SAAS:SAAS000149_004_327643][RuleBase:RU003324] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Receptor mimicry by antibody F045-092 facilitates universal binding to the H3 subtype of influenza virus.,Lee PS, Ohshima N, Stanfield RL, Yu W, Iba Y, Okuno Y, Kurosawa Y, Wilson IA Nat Commun. 2014 Apr 10;5:3614. doi: 10.1038/ncomms4614. PMID:24717798<ref>PMID:24717798</ref> | Receptor mimicry by antibody F045-092 facilitates universal binding to the H3 subtype of influenza virus.,Lee PS, Ohshima N, Stanfield RL, Yu W, Iba Y, Okuno Y, Kurosawa Y, Wilson IA Nat Commun. 2014 Apr 10;5:3614. doi: 10.1038/ncomms4614. PMID:24717798<ref>PMID:24717798</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Lee, P S | + | [[Category: Lee, P S]] |
| - | [[Category: Wilson, I A | + | [[Category: Wilson, I A]] |
[[Category: Viral fusion protein]] | [[Category: Viral fusion protein]] | ||
[[Category: Viral protein]] | [[Category: Viral protein]] | ||
[[Category: Virus attachment and entry]] | [[Category: Virus attachment and entry]] | ||
Revision as of 15:00, 25 December 2014
Crystal structure of A/Victoria/361/2011 (H3N2) influenza virus hemagglutinin
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