6hcx: Difference between revisions
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<StructureSection load='6hcx' size='340' side='right' caption='[[6hcx]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='6hcx' size='340' side='right' caption='[[6hcx]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6hcx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HCX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HCX FirstGlance]. <br> | <table><tr><td colspan='2'>[[6hcx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/I75a5 I75a5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HCX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HCX 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZMR:ZANAMIVIR'>ZMR</scene></td></tr> | </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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZMR:ZANAMIVIR'>ZMR</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=384509 I75A5])</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='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=6hcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hcx OCA], [http://pdbe.org/6hcx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hcx RCSB], [http://www.ebi.ac.uk/pdbsum/6hcx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hcx ProSAT]</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=6hcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hcx OCA], [http://pdbe.org/6hcx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hcx RCSB], [http://www.ebi.ac.uk/pdbsum/6hcx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hcx ProSAT]</span></td></tr> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Exo-alpha-sialidase]] | [[Category: Exo-alpha-sialidase]] | ||
[[Category: I75a5]] | |||
[[Category: Garman, E F]] | [[Category: Garman, E F]] | ||
[[Category: Hobbs, J R]] | [[Category: Hobbs, J R]] | ||
[[Category: Kuhn, P]] | [[Category: Kuhn, P]] | ||
[[Category: Laver, W G]] | [[Category: Laver, W G]] | ||
[[Category: Murray, J | [[Category: Murray, J W]] | ||
[[Category: Salinger, M T]] | [[Category: Salinger, M T]] | ||
[[Category: Complex]] | [[Category: Complex]] | ||
Latest revision as of 13:36, 5 September 2018
Influenza Virus N9 Neuraminidase A complex with Zanamivir molecule (Tern).Influenza Virus N9 Neuraminidase A complex with Zanamivir molecule (Tern).
Structural highlights
Function[NRAM_I75A5] 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. |
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