4o58
From Proteopedia
(Difference between revisions)
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<StructureSection load='4o58' size='340' side='right' caption='[[4o58]], [[Resolution|resolution]] 2.75Å' scene=''> | <StructureSection load='4o58' size='340' side='right' caption='[[4o58]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4o58]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/I75a3 I75a3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O58 OCA]. <br> | + | <table><tr><td colspan='2'>[[4o58]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/I75a3 I75a3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O58 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O58 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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></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=392809 I75A3]), IGL@, IGLC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=392809 I75A3]), IGL@, IGLC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4o58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o58 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o58 RCSB], [http://www.ebi.ac.uk/pdbsum/4o58 PDBsum]</span></td></tr> |
| - | + | </table> | |
| - | <table> | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/HEMA_I75A3 HEMA_I75A3]] 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. | ||
<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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[[Category: Human]] | [[Category: Human]] | ||
[[Category: I75a3]] | [[Category: I75a3]] | ||
| - | [[Category: Lee, P S | + | [[Category: Lee, P S]] |
| - | [[Category: Wilson, I A | + | [[Category: Wilson, I A]] |
[[Category: Immune recognition]] | [[Category: Immune recognition]] | ||
[[Category: Immunoglobulin]] | [[Category: Immunoglobulin]] | ||
[[Category: Viral protein-immune system complex]] | [[Category: Viral protein-immune system complex]] | ||
[[Category: Virus attachment and entry]] | [[Category: Virus attachment and entry]] | ||
Revision as of 06:20, 25 December 2014
Crystal structure of broadly neutralizing antibody F045-092 in complex with A/Victoria/3/1975 (H3N2) influenza hemagglutinin
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