4jul
From Proteopedia
(Difference between revisions)
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<StructureSection load='4jul' size='340' side='right' caption='[[4jul]], [[Resolution|resolution]] 2.79Å' scene=''> | <StructureSection load='4jul' size='340' side='right' caption='[[4jul]], [[Resolution|resolution]] 2.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4jul]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JUL OCA]. <br> | + | <table><tr><td colspan='2'>[[4jul]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JUL FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4jul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jul OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jul RCSB], [http://www.ebi.ac.uk/pdbsum/4jul PDBsum]</span></td></tr> | |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jul OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jul RCSB], [http://www.ebi.ac.uk/pdbsum/4jul PDBsum]</span></td></tr> | + | </table> |
| - | <table> | + | == Function == |
| - | == | + | [[http://www.uniprot.org/uniprot/Q00G25_9INFA Q00G25_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:SAAS000149_004_327643] |
| - | + | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Coop, T | + | [[Category: Coop, T]] |
| - | [[Category: DuBois, R M | + | [[Category: DuBois, R M]] |
| - | [[Category: Heath, R J | + | [[Category: Heath, R J]] |
| - | [[Category: Reddivari, M | + | [[Category: Reddivari, M]] |
| - | [[Category: Russell, C J | + | [[Category: Russell, C J]] |
| - | [[Category: White, S W | + | [[Category: White, S W]] |
| - | [[Category: Zaraket, H | + | [[Category: Zaraket, H]] |
[[Category: Glycosylation]] | [[Category: Glycosylation]] | ||
[[Category: Hemagglutinin]] | [[Category: Hemagglutinin]] | ||
Revision as of 03:36, 25 December 2014
Crystal structure of H5N1 influenza virus hemagglutinin, clade 2.3.4
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