4wef: Difference between revisions
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<StructureSection load='4wef' size='340' side='right'caption='[[4wef]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4wef' size='340' side='right'caption='[[4wef]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wef]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4wef]] 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=4WEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WEF 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=DF4:(3R,4R,5R,6R)-5-(ACETYLAMINO)-3-FLUORO-4-HYDROXY-6-[(1R,2R)-1,2,3-TRIHYDROXYPROPYL]-3,4,5,6-TETRAHYDROPYRANIUM-2-CARBOXYLATE'>DF4</scene>, <scene name='pdbligand=FSI:5-(ACETYLAMINO)-3,5-DIDEOXY-3-FLUORO-D-ERYTHRO-ALPHA-L-MANNO-NON-2-ULOPYRANOSONIC+ACID'>FSI</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SFJ:(2R,3R,4R,5R,6R)-5-(ACETYLAMINO)-2,3-DIFLUORO-4-HYDROXY-6-[(1R,2R)-1,2,3-TRIHYDROXYPROPYL]TETRAHYDRO-2H-PYRAN-2-CARBOXYLIC+ACID'>SFJ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | </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=DF4:(3R,4R,5R,6R)-5-(ACETYLAMINO)-3-FLUORO-4-HYDROXY-6-[(1R,2R)-1,2,3-TRIHYDROXYPROPYL]-3,4,5,6-TETRAHYDROPYRANIUM-2-CARBOXYLATE'>DF4</scene>, <scene name='pdbligand=FSI:5-(ACETYLAMINO)-3,5-DIDEOXY-3-FLUORO-D-ERYTHRO-ALPHA-L-MANNO-NON-2-ULOPYRANOSONIC+ACID'>FSI</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SFJ:(2R,3R,4R,5R,6R)-5-(ACETYLAMINO)-2,3-DIFLUORO-4-HYDROXY-6-[(1R,2R)-1,2,3-TRIHYDROXYPROPYL]TETRAHYDRO-2H-PYRAN-2-CARBOXYLIC+ACID'>SFJ</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=4wef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wef OCA], [https://pdbe.org/4wef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wef RCSB], [https://www.ebi.ac.uk/pdbsum/4wef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wef 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/Q6WJ03_9MONO Q6WJ03_9MONO] Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion.[ARBA:ARBA00025476] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human respirovirus 3]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Barrett | [[Category: Barrett S]] | ||
[[Category: McKimm-Breschkin | [[Category: McKimm-Breschkin J]] | ||
[[Category: Pilling | [[Category: Pilling P]] | ||
[[Category: Streltsov | [[Category: Streltsov VA]] | ||
Revision as of 10:04, 7 April 2023
Structure of the Hemagglutinin-neuraminidase from Human parainfluenza virus type III: complex with difluorosialic acidStructure of the Hemagglutinin-neuraminidase from Human parainfluenza virus type III: complex with difluorosialic acid
Structural highlights
FunctionQ6WJ03_9MONO Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion.[ARBA:ARBA00025476] Publication Abstract from PubMedThe human parainfluenza virus type 3 (hPIV3) hemagglutinin-neuraminidase (HN) has opposing functions of binding sialic acid receptors and cleaving them, facilitating virus release. The crystal structure of hPIV3 HN complexed with the substrate analogue difluorosialic acid (DFSA) revealed that catalysis by HN involves the formation of a covalently linked sialosyl-enzyme intermediate which was trapped along with a transition-state analogue resembling an oxocarbenium ion. This mechanism of enzyme catalysis was also confirmed in the crystal structure of the influenza N9 neuraminidase complexed with DFSA. Additionally, novel secondary receptor binding sites were identified in the hPIV3 HN-DFSA complex including one near the catalytic cavity which upon binding DFSA imposes subtle changes and may help the HN balance the opposing functions. Multiple receptor binding sites may increase avidity to facilitate cell binding and fusion promotion. The secondary receptor binding sites in the paramyxoviruses are so far unique to each virus type. Catalytic mechanism and novel receptor binding sites of human parainfluenza virus type 3 hemagglutinin-neuraminidase (hPIV3 HN).,Streltsov VA, Pilling P, Barrett S, McKimm-Breschkin JL Antiviral Res. 2015 Sep 10. pii: S0166-3542(15)00209-0. doi:, 10.1016/j.antiviral.2015.08.014. PMID:26364554[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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