View source for 2vsm


==Nipah virus attachment glycoprotein in complex with human cell surface receptor ephrinB2==
<StructureSection load='2vsm' size='340' side='right'caption='[[2vsm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vsm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Henipavirus_nipahense Henipavirus nipahense] 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=2VSM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VSM 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=2vsm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vsm OCA], [https://pdbe.org/2vsm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vsm RCSB], [https://www.ebi.ac.uk/pdbsum/2vsm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vsm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EFNB2_HUMAN EFNB2_HUMAN] Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds to receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4. Together with EPHB4 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells. May play a role in constraining the orientation of longitudinally projecting axons.<ref>PMID:12734395</ref> 
== 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/vs/2vsm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2vsm ConSurf].
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== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2vsm" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ephrin|Ephrin]]
*[[Ephrin receptor 3D structures|Ephrin receptor 3D structures]]
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Henipavirus nipahense]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Aricescu AR]]
[[Category: Bowden TA]]
[[Category: Gilbert RJ]]
[[Category: Grimes JM]]
[[Category: Jones EY]]
[[Category: Stuart DI]]