2vsk

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[[Image:2vsk.png|left|200px]]
 
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{{STRUCTURE_2vsk| PDB=2vsk | SCENE= }}
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==Hendra virus attachment glycoprotein in complex with human cell surface receptor ephrinB2==
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<StructureSection load='2vsk' size='340' side='right'caption='[[2vsk]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2vsk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Hendra_henipavirus Hendra henipavirus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VSK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VSK FirstGlance]. <br>
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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]] 3.3&#8491;</td></tr>
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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=2vsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vsk OCA], [https://pdbe.org/2vsk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vsk RCSB], [https://www.ebi.ac.uk/pdbsum/2vsk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vsk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLYCP_HENDH GLYCP_HENDH] Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of glycoprotein G to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (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/vs/2vsk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2vsk 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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Nipah and Hendra viruses are emergent paramyxoviruses, causing disease characterized by rapid onset and high mortality rates, resulting in their classification as Biosafety Level 4 pathogens. Their attachment glycoproteins are essential for the recognition of the cell-surface receptors ephrin-B2 (EFNB2) and ephrin-B3 (EFNB3). Here we report crystal structures of both Nipah and Hendra attachment glycoproteins in complex with human EFNB2. In contrast to previously solved paramyxovirus attachment complexes, which are mediated by sialic acid interactions, the Nipah and Hendra complexes are maintained by an extensive protein-protein interface, including a crucial phenylalanine side chain on EFNB2 that fits snugly into a hydrophobic pocket on the viral protein. By analogy with the development of antivirals against sialic acid binding viruses, these results provide a structural template to target antiviral inhibition of protein-protein interactions.
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===HENDRA VIRUS ATTACHMENT GLYCOPROTEIN IN COMPLEX WITH HUMAN CELL SURFACE RECEPTOR EPHRINB2===
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Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2.,Bowden TA, Aricescu AR, Gilbert RJ, Grimes JM, Jones EY, Stuart DI Nat Struct Mol Biol. 2008 Jun;15(6):567-72. Epub 2008 May 18. PMID:18488039<ref>PMID:18488039</ref>
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{{ABSTRACT_PUBMED_18488039}}
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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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==About this Structure==
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<div class="pdbe-citations 2vsk" style="background-color:#fffaf0;"></div>
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[[2vsk]] is a 4 chain structure of [[Ephrin receptor]] and [[Hemagglutinin]] with sequence from [http://en.wikipedia.org/wiki/Hendra_virus Hendra virus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VSK OCA].
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==See Also==
==See Also==
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*[[Ephrin receptor|Ephrin receptor]]
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*[[Ephrin|Ephrin]]
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*[[Hemagglutinin|Hemagglutinin]]
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*[[Ephrin receptor 3D structures|Ephrin receptor 3D structures]]
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:018488039</ref><references group="xtra"/>
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<references/>
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[[Category: Exo-alpha-sialidase]]
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__TOC__
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[[Category: Hendra virus]]
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</StructureSection>
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[[Category: Hendra henipavirus]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Aricescu, A R.]]
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[[Category: Large Structures]]
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[[Category: Bowden, T A.]]
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[[Category: Aricescu AR]]
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[[Category: Gilbert, R J.]]
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[[Category: Bowden TA]]
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[[Category: Grimes, J M.]]
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[[Category: Gilbert RJ]]
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[[Category: Jones, E Y.]]
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[[Category: Grimes JM]]
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[[Category: Stuart, D I.]]
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[[Category: Jones EY]]
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[[Category: B2]]
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[[Category: Stuart DI]]
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[[Category: Cell surface receptor]]
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[[Category: Complex]]
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[[Category: Developmental protein]]
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[[Category: Differentiation]]
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[[Category: Efn]]
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[[Category: Envelope protein]]
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[[Category: Eph]]
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[[Category: Ephrin]]
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[[Category: Glycoprotein]]
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[[Category: Hemagglutinin]]
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[[Category: Hendra]]
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[[Category: Henipavirus]]
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[[Category: Hev]]
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[[Category: Hev-g]]
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[[Category: Hydrolase]]
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[[Category: Membrane]]
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[[Category: Neurogenesis]]
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[[Category: Nipah]]
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[[Category: Niv]]
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[[Category: Niv-g]]
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[[Category: Paramyxovirus]]
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[[Category: Phosphoprotein]]
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[[Category: Signal-anchor]]
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[[Category: Transmembrane]]
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[[Category: Viral attachment]]
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[[Category: Virion]]
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[[Category: Virus]]
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Current revision

Hendra virus attachment glycoprotein in complex with human cell surface receptor ephrinB2

PDB ID 2vsk

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