4o5i
From Proteopedia
(Difference between revisions)
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==Crystal structure of broadly neutralizing antibody F045-092 in complex with A/Victoria/361/2011 (H3N2) influenza hemagglutinin== | ==Crystal structure of broadly neutralizing antibody F045-092 in complex with A/Victoria/361/2011 (H3N2) influenza hemagglutinin== | ||
<StructureSection load='4o5i' size='340' side='right' caption='[[4o5i]], [[Resolution|resolution]] 6.50Å' scene=''> | <StructureSection load='4o5i' size='340' side='right' caption='[[4o5i]], [[Resolution|resolution]] 6.50Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o58|4o58]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o58|4o58]]</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))]), 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=1331560 Influenza A virus (A/Singapore/H2011.447/2011(H3N2))]), IGL@, IGLC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4o5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o5i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o5i RCSB], [http://www.ebi.ac.uk/pdbsum/4o5i PDBsum]</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=4o5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o5i OCA], [http://pdbe.org/4o5i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o5i RCSB], [http://www.ebi.ac.uk/pdbsum/4o5i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o5i ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | {{Large structure}} | ||
== Function == | == 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] | [[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] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 4o5i" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Hemagglutinin|Hemagglutinin]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 22:52, 5 August 2016
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Crystal structure of broadly neutralizing antibody F045-092 in complex with A/Victoria/361/2011 (H3N2) influenza hemagglutinin
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