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<StructureSection load='1e8u' size='340' side='right'caption='[[1e8u]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1e8u' size='340' side='right'caption='[[1e8u]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1e8u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Newcastle_disease_virus Newcastle disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E8U FirstGlance]. <br>
<table><tr><td colspan='2'>[[1e8u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Avian_orthoavulavirus_1 Avian orthoavulavirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E8U FirstGlance]. <br>
</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SLB:5-N-ACETYL-BETA-D-NEURAMINIC+ACID'>SLB</scene></td></tr>
</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&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e8t|1e8t]], [[1e8v|1e8v]]</div></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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SLB:5-N-ACETYL-BETA-D-NEURAMINIC+ACID'>SLB</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=1e8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8u OCA], [https://pdbe.org/1e8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e8u RCSB], [https://www.ebi.ac.uk/pdbsum/1e8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e8u ProSAT]</span></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=1e8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8u OCA], [https://pdbe.org/1e8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e8u RCSB], [https://www.ebi.ac.uk/pdbsum/1e8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e8u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HN_NDVK HN_NDVK]] 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 (By similarity).  Neuraminidase activity ensures the efficient spread of the virus by dissociating the mature virions from the neuraminic acid containing glycoproteins (By similarity).  
[https://www.uniprot.org/uniprot/HN_NDVK HN_NDVK] 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 (By similarity).  Neuraminidase activity ensures the efficient spread of the virus by dissociating the mature virions from the neuraminic acid containing glycoproteins (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1e8u ConSurf].
</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=1e8u ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Paramyxoviruses are the main cause of respiratory disease in children. One of two viral surface glycoproteins, the hemagglutinin-neuraminidase (HN), has several functions in addition to being the major surface antigen that induces neutralizing antibodies. Here we present the crystal structures of Newcastle disease virus HN alone and in complex with either an inhibitor or with the beta-anomer of sialic acid. The inhibitor complex reveals a typical neuraminidase active site within a beta-propeller fold. Comparison of the structures of the two complexes reveal differences in the active site, suggesting that the catalytic site is activated by a conformational switch. This site may provide both sialic acid binding and hydrolysis functions since there is no evidence for a second sialic acid binding site in HN. Evidence for a single site with dual functions is examined and supported by mutagenesis studies. The structure provides the basis for the structure-based design of inhibitors for a range of paramyxovirus-induced diseases.
Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase.,Crennell S, Takimoto T, Portner A, Taylor G Nat Struct Biol. 2000 Nov;7(11):1068-74. PMID:11062565<ref>PMID:11062565</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1e8u" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Exo-alpha-sialidase]]
[[Category: Avian orthoavulavirus 1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Newcastle disease virus]]
[[Category: Crennell S]]
[[Category: Crennell, S]]
[[Category: Portner A]]
[[Category: Portner, A]]
[[Category: Takimoto T]]
[[Category: Takimoto, T]]
[[Category: Taylor G]]
[[Category: Taylor, G]]
[[Category: Hemagglutinin]]
[[Category: Hydrolase]]
[[Category: Neuraminidase]]
[[Category: Sialidase]]

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