2hu0: Difference between revisions
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<StructureSection load='2hu0' size='340' side='right'caption='[[2hu0]], [[Resolution|resolution]] 2.95Å' scene=''> | <StructureSection load='2hu0' size='340' side='right'caption='[[2hu0]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2hu0]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2hu0]] is a 8 chain structure with sequence from [https://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=2HU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HU0 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G39:(3R,4R,5S)-4-(ACETYLAMINO)-5-AMINO-3-(PENTAN-3-YLOXY)CYCLOHEX-1-ENE-1-CARBOXYLIC+ACID'>G39</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G39:(3R,4R,5S)-4-(ACETYLAMINO)-5-AMINO-3-(PENTAN-3-YLOXY)CYCLOHEX-1-ENE-1-CARBOXYLIC+ACID'>G39</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ht5|2ht5]], [[2ht7|2ht7]], [[2ht8|2ht8]], [[2htu|2htu]], [[2htq|2htq]], [[2htv|2htv]], [[2htw|2htw]], [[2hty|2hty]], [[2htr|2htr]], [[2hu4|2hu4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ht5|2ht5]], [[2ht7|2ht7]], [[2ht8|2ht8]], [[2htu|2htu]], [[2htq|2htq]], [[2htv|2htv]], [[2htw|2htw]], [[2hty|2hty]], [[2htr|2htr]], [[2hu4|2hu4]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu0 OCA], [https://pdbe.org/2hu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hu0 RCSB], [https://www.ebi.ac.uk/pdbsum/2hu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hu0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/Q6DPL2_9INFA Q6DPL2_9INFA]] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates.[RuleBase:RU361252] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[ | *[[Neuraminidase 3D structures|Neuraminidase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 20:46, 20 October 2021
N1 neuraminidase in complex with oseltamivir 1N1 neuraminidase in complex with oseltamivir 1
Structural highlights
Function[Q6DPL2_9INFA] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates.[RuleBase:RU361252] Publication Abstract from PubMedThe worldwide spread of H5N1 avian influenza has raised concerns that this virus might acquire the ability to pass readily among humans and cause a pandemic. Two anti-influenza drugs currently being used to treat infected patients are oseltamivir (Tamiflu) and zanamivir (Relenza), both of which target the neuraminidase enzyme of the virus. Reports of the emergence of drug resistance make the development of new anti-influenza molecules a priority. Neuraminidases from influenza type A viruses form two genetically distinct groups: group-1 contains the N1 neuraminidase of the H5N1 avian virus and group-2 contains the N2 and N9 enzymes used for the structure-based design of current drugs. Here we show by X-ray crystallography that these two groups are structurally distinct. Group-1 neuraminidases contain a cavity adjacent to their active sites that closes on ligand binding. Our analysis suggests that it may be possible to exploit the size and location of the group-1 cavity to develop new anti-influenza drugs. The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design.,Russell RJ, Haire LF, Stevens DJ, Collins PJ, Lin YP, Blackburn GM, Hay AJ, Gamblin SJ, Skehel JJ Nature. 2006 Sep 7;443(7107):45-9. Epub 2006 Aug 16. PMID:16915235[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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