6q23
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human 1G01 Fab in complex with influenza virus neuraminidase from A/California/04/2009 (H1N1)== | |
| - | + | <StructureSection load='6q23' size='340' side='right'caption='[[6q23]], [[Resolution|resolution]] 3.27Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6q23]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q23 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q23 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </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=6q23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q23 OCA], [http://pdbe.org/6q23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q23 RCSB], [http://www.ebi.ac.uk/pdbsum/6q23 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q23 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/C5MQL2_9INFA C5MQL2_9INFA]] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.[HAMAP-Rule:MF_04071][SAAS:SAAS00844152] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Exo-alpha-sialidase]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Wilson, I A]] | ||
| + | [[Category: Zhu, X]] | ||
| + | [[Category: Active site]] | ||
| + | [[Category: Antibody-neuraminidase complex]] | ||
| + | [[Category: Broadly protective human antibody]] | ||
| + | [[Category: Hydrolase-immune system complex]] | ||
| + | [[Category: Inhibition]] | ||
| + | [[Category: Viral protein]] | ||
Revision as of 07:01, 23 October 2019
Crystal structure of human 1G01 Fab in complex with influenza virus neuraminidase from A/California/04/2009 (H1N1)
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