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==The catalytic mechanism of human parainfluenza virus type 3 haemagglutinin-neuraminidase revealed== | ==The catalytic mechanism of human parainfluenza virus type 3 haemagglutinin-neuraminidase revealed== | ||
<StructureSection load='4xjq' size='340' side='right' caption='[[4xjq]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4xjq' size='340' side='right'caption='[[4xjq]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xjq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XJQ OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4xjq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_respirovirus_3 Human respirovirus 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XJQ 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4xjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xjq OCA], [https://pdbe.org/4xjq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xjq RCSB], [https://www.ebi.ac.uk/pdbsum/4xjq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xjq ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/G8G134_9MONO G8G134_9MONO] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 4xjq" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4xjq" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human respirovirus 3]] | ||
[[Category: Carroux | [[Category: Large Structures]] | ||
[[Category: Chavas | [[Category: Carroux C]] | ||
[[Category: Dirr | [[Category: Chavas L]] | ||
[[Category: El-Deeb | [[Category: Dirr L]] | ||
[[Category: Guillon | [[Category: El-Deeb I]] | ||
[[Category: Itzstein | [[Category: Guillon P]] | ||
[[Category: Von Itzstein M]] | |||
Latest revision as of 10:46, 27 September 2023
The catalytic mechanism of human parainfluenza virus type 3 haemagglutinin-neuraminidase revealedThe catalytic mechanism of human parainfluenza virus type 3 haemagglutinin-neuraminidase revealed
Structural highlights
FunctionPublication Abstract from PubMedHuman parainfluenza virus type 3 (hPIV-3) is one of the leading causes for lower respiratory tract disease in children, with neither an approved antiviral drug nor vaccine available to date. Understanding the catalytic mechanism of human parainfluenza virus haemagglutinin-neuraminidase (HN) protein is key to the design of specific inhibitors against this virus. Herein, we used (1) H NMR spectroscopy, X-ray crystallography, and virological assays to study the catalytic mechanism of the HN enzyme activity and have identified the conserved Tyr530 as a key amino acid involved in catalysis. A novel 2,3-difluorosialic acid derivative showed prolonged enzyme inhibition and was found to react and form a covalent bond with Tyr530. Furthermore, the novel derivative exhibited enhanced potency in virus blockade assays relative to its Neu2en analogue. These outcomes open the door for a new generation of potent inhibitors against hPIV-3 HN. The catalytic mechanism of human parainfluenza virus type 3 haemagglutinin-neuraminidase revealed.,Dirr L, El-Deeb IM, Guillon P, Carroux CJ, Chavas LM, von Itzstein M Angew Chem Int Ed Engl. 2015 Mar 2;54(10):2936-40. doi: 10.1002/anie.201412243., Epub 2015 Feb 10. PMID:25676091[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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