|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4d8s' size='340' side='right'caption='[[4d8s]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='4d8s' size='340' side='right'caption='[[4d8s]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d8s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D8S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4D8S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d8s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/duck/Ukraine/1/1963(H3N8)) Influenza A virus (A/duck/Ukraine/1/1963(H3N8))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D8S FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0HX:PENTAN-3-YL+2-(ACETYLAMINO)-2,4-DIDEOXY-ALPHA-L-THREO-HEX-4-ENOPYRANOSIDURONIC+ACID'>0HX</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0HX:PENTAN-3-YL+2-(ACETYLAMINO)-2,4-DIDEOXY-ALPHA-L-THREO-HEX-4-ENOPYRANOSIDURONIC+ACID'>0HX</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <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'>[https://proteopedia.org/fgij/fg.htm?mol=4d8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d8s OCA], [https://pdbe.org/4d8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d8s RCSB], [https://www.ebi.ac.uk/pdbsum/4d8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d8s ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4d8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d8s OCA], [http://pdbe.org/4d8s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d8s RCSB], [http://www.ebi.ac.uk/pdbsum/4d8s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d8s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NRAM_I63A3 NRAM_I63A3]] 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. | + | [[https://www.uniprot.org/uniprot/NRAM_I63A3 NRAM_I63A3]] 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 25: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Exo-alpha-sialidase]] | |
| - | [[Category: Influenza a virus]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kerry, P S]] | + | [[Category: Kerry PS]] |
| - | [[Category: Russell, R J.M R]] | + | [[Category: Russell RJMR]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Neuraminidase]]
| + | |
| Structural highlights
Function
[NRAM_I63A3] 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.
Publication Abstract from PubMed
A series of C3 O-functionalized 2-acetamido-2-deoxy-Delta(4)-beta-D-glucuronides were synthesized to explore noncharge interactions in subsite 2 of the influenza virus sialidase active site. In complex with A/N8 sialidase, the parent compound (C3 OH) inverts its solution conformation to bind with all substituents well positioned in the active site. The parent compound inhibits influenza virus sialidase at a sub-muM level; the introduction of small alkyl substituents or an acetyl group at C3 is also tolerated.
Exploring the interactions of unsaturated glucuronides with influenza virus sialidase.,Bhatt B, Bohm R, Kerry PS, Dyason JC, Russell RJ, Thomson RJ, von Itzstein M J Med Chem. 2012 Oct 25;55(20):8963-8. doi: 10.1021/jm301145k. Epub 2012 Oct 11. PMID:23017008[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bhatt B, Bohm R, Kerry PS, Dyason JC, Russell RJ, Thomson RJ, von Itzstein M. Exploring the interactions of unsaturated glucuronides with influenza virus sialidase. J Med Chem. 2012 Oct 25;55(20):8963-8. doi: 10.1021/jm301145k. Epub 2012 Oct 11. PMID:23017008 doi:http://dx.doi.org/10.1021/jm301145k
|
