|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6p7y' size='340' side='right'caption='[[6p7y]], [[Resolution|resolution]] 2.84Å' scene=''> | | <StructureSection load='6p7y' size='340' side='right'caption='[[6p7y]], [[Resolution|resolution]] 2.84Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6p7y]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cedpv Cedpv] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P7Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P7Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6p7y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cedar_virus Cedar virus] 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=6P7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P7Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.844Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EFNB2, EPLG5, HTKL, LERK5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6p7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p7y OCA], [http://pdbe.org/6p7y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p7y RCSB], [http://www.ebi.ac.uk/pdbsum/6p7y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p7y 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=6p7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p7y OCA], [https://pdbe.org/6p7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p7y RCSB], [https://www.ebi.ac.uk/pdbsum/6p7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p7y ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [https://www.uniprot.org/uniprot/J7H333_9MONO J7H333_9MONO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 19: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6p7y" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6p7y" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ephrin|Ephrin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cedpv]] | |
| - | [[Category: Human]] | |
| - | [[Category: Large Structures]] | |
| - | [[Category: Nikolov, D B]] | |
| - | [[Category: Xu, K]] | |
| - | [[Category: Xu, Y]] | |
| - | [[Category: Attachment]] | |
| | [[Category: Cedar virus]] | | [[Category: Cedar virus]] |
| - | [[Category: Ephrin-b2]] | + | [[Category: Homo sapiens]] |
| - | [[Category: G protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Glycoprotein]] | + | [[Category: Nikolov DB]] |
| - | [[Category: Henipavirus]] | + | [[Category: Xu K]] |
| - | [[Category: Receptor]] | + | [[Category: Xu Y]] |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
J7H333_9MONO
Publication Abstract from PubMed
Cedar virus (CedV) is a bat-borne henipavirus related to Nipah virus (NiV) and Hendra virus (HeV), zoonotic agents of fatal human disease. CedV receptor-binding protein (G) shares only approximately 30% sequence identity with those of NiV and HeV, although they can all use ephrin-B2 as an entry receptor. We demonstrate that CedV also enters cells through additional B- and A-class ephrins (ephrin-B1, ephrin-A2, and ephrin-A5) and report the crystal structure of the CedV G ectodomain alone and in complex with ephrin-B1 or ephrin-B2. The CedV G receptor-binding site is structurally distinct from other henipaviruses, underlying its capability to accommodate additional ephrin receptors. We also show that CedV can enter cells through mouse ephrin-A1 but not human ephrin-A1, which differ by 1 residue in the key contact region. This is evidence of species specific ephrin receptor usage by a henipavirus, and implicates additional ephrin receptors in potential zoonotic transmission.
Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus.,Laing ED, Navaratnarajah CK, Cheliout Da Silva S, Petzing SR, Xu Y, Sterling SL, Marsh GA, Wang LF, Amaya M, Nikolov DB, Cattaneo R, Broder CC, Xu K Proc Natl Acad Sci U S A. 2019 Oct 8;116(41):20707-20715. doi:, 10.1073/pnas.1911773116. Epub 2019 Sep 23. PMID:31548390[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Laing ED, Navaratnarajah CK, Cheliout Da Silva S, Petzing SR, Xu Y, Sterling SL, Marsh GA, Wang LF, Amaya M, Nikolov DB, Cattaneo R, Broder CC, Xu K. Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus. Proc Natl Acad Sci U S A. 2019 Oct 8;116(41):20707-20715. doi:, 10.1073/pnas.1911773116. Epub 2019 Sep 23. PMID:31548390 doi:http://dx.doi.org/10.1073/pnas.1911773116
|
