1e8v

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[[Image:1e8v.png|left|200px]]
 
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==Structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase==
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The line below this paragraph, containing "STRUCTURE_1e8v", creates the "Structure Box" on the page.
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<StructureSection load='1e8v' size='340' side='right'caption='[[1e8v]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1e8v]] 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=1E8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E8V FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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></td></tr>
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{{STRUCTURE_1e8v| PDB=1e8v | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8v OCA], [https://pdbe.org/1e8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e8v RCSB], [https://www.ebi.ac.uk/pdbsum/1e8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e8v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e8/1e8v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1e8v ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS HEMAGGLUTININ-NEURAMINIDASE===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1e8v" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11062565}}, adds the Publication Abstract to the page
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11062565 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11062565}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Avian orthoavulavirus 1]]
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[[1e8v]] is a 2 chain structure with sequence from [http://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=1E8V OCA].
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[[Category: Large Structures]]
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[[Category: Crennell S]]
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==Reference==
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[[Category: Portner A]]
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<ref group="xtra">PMID:11062565</ref><ref group="xtra">PMID:10772993</ref><references group="xtra"/>
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[[Category: Takimoto T]]
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[[Category: Exo-alpha-sialidase]]
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[[Category: Taylor G]]
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[[Category: Newcastle disease virus]]
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[[Category: Crennell, S.]]
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[[Category: Portner, A.]]
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[[Category: Takimoto, T.]]
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[[Category: Taylor, G.]]
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[[Category: Hemagglutinin]]
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[[Category: Hemagglutinin-neuraminidase]]
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[[Category: Neuraminidase]]
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[[Category: Sialidase]]
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Current revision

Structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase

PDB ID 1e8v

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