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2vsk

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<StructureSection load='2vsk' size='340' side='right'caption='[[2vsk]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='2vsk' size='340' side='right'caption='[[2vsk]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2vsk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Equine_morbillivirus Equine morbillivirus] and [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VSK FirstGlance]. <br>
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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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vsm|2vsm]]</td></tr>
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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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </span></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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vsk OCA], [http://pdbe.org/2vsk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vsk RCSB], [http://www.ebi.ac.uk/pdbsum/2vsk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vsk ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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). [[http://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>
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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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Equine morbillivirus]]
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[[Category: Hendra henipavirus]]
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[[Category: Exo-alpha-sialidase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Aricescu, A R]]
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[[Category: Aricescu AR]]
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[[Category: Bowden, T A]]
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[[Category: Bowden TA]]
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[[Category: Gilbert, R J]]
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[[Category: Gilbert RJ]]
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[[Category: Grimes, J M]]
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[[Category: Grimes JM]]
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[[Category: Jones, E Y]]
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[[Category: Jones EY]]
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[[Category: Stuart, D I]]
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[[Category: Stuart DI]]
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[[Category: B2]]
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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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OCA

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