6aoq
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of the A/Brisbane/10/2007 (H3N2) influenza virus hemagglutinin apo form== | |
- | + | <StructureSection load='6aoq' size='340' side='right' caption='[[6aoq]], [[Resolution|resolution]] 2.35Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[6aoq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AOQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AOQ 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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |
- | [[Category: | + | <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=6aoq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aoq OCA], [http://pdbe.org/6aoq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aoq RCSB], [http://www.ebi.ac.uk/pdbsum/6aoq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aoq ProSAT]</span></td></tr> |
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/A8W891_9INFA A8W891_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 either through clathrin-dependent endocytosis or through 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.[SAAS:SAAS00842036] 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.[RuleBase:RU003324] | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Wilson, I A]] | ||
+ | [[Category: Wu, N C]] | ||
+ | [[Category: Antigenicity]] | ||
+ | [[Category: Hemagglutinin]] | ||
+ | [[Category: Influenza a virus]] | ||
+ | [[Category: Mutant]] | ||
+ | [[Category: Receptor binding]] | ||
+ | [[Category: Viral protein]] |
Revision as of 07:20, 18 October 2017
Crystal structure of the A/Brisbane/10/2007 (H3N2) influenza virus hemagglutinin apo form
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