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==Structure of the hemagglutinin-neuraminidase from human parainfluenza virus type III: complex with NEU5AC2EN== | |||
<StructureSection load='1v3d' size='340' side='right'caption='[[1v3d]], [[Resolution|resolution]] 2.28Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1v3d]] 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=1V3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V3D FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DAN:2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC+ACID'>DAN</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=1v3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v3d OCA], [https://pdbe.org/1v3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v3d RCSB], [https://www.ebi.ac.uk/pdbsum/1v3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v3d ProSAT]</span></td></tr> | |||
</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] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v3/1v3d_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1v3d ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The three-dimensional structure of the haemagglutinin-neuraminidase (HN) from a human parainfluenza virus is described at ca 2.0 A resolution, both in native form and in complex with three substrate analogues. In support of earlier work on the structure of the homologous protein from the avian pathogen Newcastle disease virus (NDV), we observe a dimer of beta-propellers and find no evidence for spatially separated sites performing the receptor-binding and neuraminidase functions of the protein. As with the NDV HN, the active site of the HN of parainfluenza viruses is structurally flexible, suggesting that it may be able to switch between a receptor-binding state and a catalytic state. However, in contrast to the NDV structures, we observe no ligand-induced structural changes that extend beyond the active site and modify the dimer interface. | |||
Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III.,Lawrence MC, Borg NA, Streltsov VA, Pilling PA, Epa VC, Varghese JN, McKimm-Breschkin JL, Colman PM J Mol Biol. 2004 Jan 30;335(5):1343-57. PMID:14729348<ref>PMID:14729348</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1v3d" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]] | |||
[ | == References == | ||
[[Category: Human | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Borg | </StructureSection> | ||
[[Category: Colman | [[Category: Human respirovirus 3]] | ||
[[Category: Epa | [[Category: Large Structures]] | ||
[[Category: Lawrence | [[Category: Borg NA]] | ||
[[Category: McKimm-Breschkin | [[Category: Colman PM]] | ||
[[Category: Pilling | [[Category: Epa VC]] | ||
[[Category: Streltsov | [[Category: Lawrence MC]] | ||
[[Category: Varghese | [[Category: McKimm-Breschkin JL]] | ||
[[Category: Pilling PA]] | |||
[[Category: Streltsov VA]] | |||
[[Category: Varghese JN]] | |||
Latest revision as of 10:44, 25 October 2023
Structure of the hemagglutinin-neuraminidase from human parainfluenza virus type III: complex with NEU5AC2ENStructure of the hemagglutinin-neuraminidase from human parainfluenza virus type III: complex with NEU5AC2EN
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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe three-dimensional structure of the haemagglutinin-neuraminidase (HN) from a human parainfluenza virus is described at ca 2.0 A resolution, both in native form and in complex with three substrate analogues. In support of earlier work on the structure of the homologous protein from the avian pathogen Newcastle disease virus (NDV), we observe a dimer of beta-propellers and find no evidence for spatially separated sites performing the receptor-binding and neuraminidase functions of the protein. As with the NDV HN, the active site of the HN of parainfluenza viruses is structurally flexible, suggesting that it may be able to switch between a receptor-binding state and a catalytic state. However, in contrast to the NDV structures, we observe no ligand-induced structural changes that extend beyond the active site and modify the dimer interface. Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III.,Lawrence MC, Borg NA, Streltsov VA, Pilling PA, Epa VC, Varghese JN, McKimm-Breschkin JL, Colman PM J Mol Biol. 2004 Jan 30;335(5):1343-57. PMID:14729348[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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