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4xnm
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Antibody Influenza H5 Complex== |
| - | + | <StructureSection load='4xnm' size='340' side='right' caption='[[4xnm]], [[Resolution|resolution]] 2.51Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4xnm]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XNM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XNM FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xnq|4xnq]], [[4xrc|4xrc]]</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=4xnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xnm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xnm RCSB], [http://www.ebi.ac.uk/pdbsum/4xnm PDBsum]</span></td></tr> | |
| - | [[Category: | + | </table> |
| - | [[Category: Winarski, K | + | == Function == |
| - | [[Category: | + | [[http://www.uniprot.org/uniprot/H8PCX0_9INFA H8PCX0_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.[RuleBase:RU003324] 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:SAAS00204388] |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Spiler, B W]] | ||
| + | [[Category: Winarski, K L]] | ||
| + | [[Category: Antibody]] | ||
| + | [[Category: Influenza]] | ||
| + | [[Category: Neutralization]] | ||
| + | [[Category: Viral protein-immune system complex]] | ||
Revision as of 13:35, 15 July 2015
Antibody Influenza H5 Complex
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