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==Neuraminidase of A/Brevig Mission/1/1918 H1N1 strain in complex with zanamivir== | |||
===Neuraminidase of A/Brevig Mission/1/ | <StructureSection load='3b7e' size='340' side='right' caption='[[3b7e]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3b7e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. The May 2009 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Influenza Neuraminidase'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2009_5 10.2210/rcsb_pdb/mom_2009_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3B7E 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZMR:ZANAMIVIR'>ZMR</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3beq|3beq]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Neuraminidase ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11320 Influenza A virus])</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=3b7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b7e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3b7e RCSB], [http://www.ebi.ac.uk/pdbsum/3b7e PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Influenza virus neuraminidase (NA) plays a crucial role in facilitating the spread of newly synthesized virus in the host and is an important target for controlling disease progression. The NA crystal structure from the 1918 "Spanish flu" (A/Brevig Mission/1/18 H1N1) and that of its complex with zanamivir (Relenza) at 1.65-A and 1.45-A resolutions, respectively, corroborated the successful expression of correctly folded NA tetramers in a baculovirus expression system. An additional cavity adjacent to the substrate-binding site is observed in N1, compared to N2 and N9 NAs, including H5N1. This cavity arises from an open conformation of the 150 loop (Gly147 to Asp151) and appears to be conserved among group 1 NAs (N1, N4, N5, and N8). It closes upon zanamivir binding. Three calcium sites were identified, including a novel site that may be conserved in N1 and N4. Thus, these high-resolution structures, combined with our recombinant expression system, provide new opportunities to augment the limited arsenal of therapeutics against influenza. | |||
Structural characterization of the 1918 influenza virus H1N1 neuraminidase.,Xu X, Zhu X, Dwek RA, Stevens J, Wilson IA J Virol. 2008 Nov;82(21):10493-501. Epub 2008 Aug 20. PMID:18715929<ref>PMID:18715929</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
| Line 10: | Line 22: | ||
*[[Teaching Scenes%2C Tutorials%2C and Educators' Pages|Teaching Scenes%2C Tutorials%2C and Educators' Pages]] | *[[Teaching Scenes%2C Tutorials%2C and Educators' Pages|Teaching Scenes%2C Tutorials%2C and Educators' Pages]] | ||
*[[Zanamivir|Zanamivir]] | *[[Zanamivir|Zanamivir]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Exo-alpha-sialidase]] | [[Category: Exo-alpha-sialidase]] | ||
[[Category: Influenza Neuraminidase]] | [[Category: Influenza Neuraminidase]] | ||
[[Category: Influenza a virus]] | [[Category: Influenza a virus]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: Wilson, I A | [[Category: Wilson, I A]] | ||
[[Category: Xu, X | [[Category: Xu, X]] | ||
[[Category: Zhu, X | [[Category: Zhu, X]] | ||
[[Category: 6-bladed beta-propeller]] | [[Category: 6-bladed beta-propeller]] | ||
[[Category: Glycosidase]] | [[Category: Glycosidase]] | ||
Revision as of 17:05, 17 December 2014
Neuraminidase of A/Brevig Mission/1/1918 H1N1 strain in complex with zanamivirNeuraminidase of A/Brevig Mission/1/1918 H1N1 strain in complex with zanamivir
Structural highlights
Publication Abstract from PubMedInfluenza virus neuraminidase (NA) plays a crucial role in facilitating the spread of newly synthesized virus in the host and is an important target for controlling disease progression. The NA crystal structure from the 1918 "Spanish flu" (A/Brevig Mission/1/18 H1N1) and that of its complex with zanamivir (Relenza) at 1.65-A and 1.45-A resolutions, respectively, corroborated the successful expression of correctly folded NA tetramers in a baculovirus expression system. An additional cavity adjacent to the substrate-binding site is observed in N1, compared to N2 and N9 NAs, including H5N1. This cavity arises from an open conformation of the 150 loop (Gly147 to Asp151) and appears to be conserved among group 1 NAs (N1, N4, N5, and N8). It closes upon zanamivir binding. Three calcium sites were identified, including a novel site that may be conserved in N1 and N4. Thus, these high-resolution structures, combined with our recombinant expression system, provide new opportunities to augment the limited arsenal of therapeutics against influenza. Structural characterization of the 1918 influenza virus H1N1 neuraminidase.,Xu X, Zhu X, Dwek RA, Stevens J, Wilson IA J Virol. 2008 Nov;82(21):10493-501. Epub 2008 Aug 20. PMID:18715929[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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