6fyt
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure of H1 (A/solomon Islands/3/06) Influenza Hemagglutinin in complex with SD38== | |
| - | + | <StructureSection load='6fyt' size='340' side='right' caption='[[6fyt]], [[Resolution|resolution]] 2.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6fyt]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FYT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FYT 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=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <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=6fyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fyt OCA], [http://pdbe.org/6fyt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fyt RCSB], [http://www.ebi.ac.uk/pdbsum/6fyt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fyt ProSAT]</span></td></tr> |
| - | [[ | + | </table> |
| - | [[Category: Laursen, N | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/A7Y8I1_9INFA A7Y8I1_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.[HAMAP-Rule:MF_04072][SAAS:SAAS01039073] 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: Laursen, N S]] | ||
| + | [[Category: Wilson, I A]] | ||
| + | [[Category: Hemagglutinin]] | ||
| + | [[Category: Influenza]] | ||
| + | [[Category: Single domain antibody]] | ||
| + | [[Category: Viral protein]] | ||
Revision as of 12:17, 7 November 2018
Structure of H1 (A/solomon Islands/3/06) Influenza Hemagglutinin in complex with SD38
| |||||||||||
