|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6thg' size='340' side='right'caption='[[6thg]], [[Resolution|resolution]] 4.07Å' scene=''> | | <StructureSection load='6thg' size='340' side='right'caption='[[6thg]], [[Resolution|resolution]] 4.07Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6thg]] is a 10 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=6THG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6THG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6thg]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Cedpv Cedpv] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6THG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6THG 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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6thb|6thb]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6thb|6thb]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EFNB1, EFL3, EPLG2, LERK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EFNB1, EFL3, EPLG2, LERK2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6thg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6thg OCA], [http://pdbe.org/6thg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6thg RCSB], [http://www.ebi.ac.uk/pdbsum/6thg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6thg 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=6thg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6thg OCA], [https://pdbe.org/6thg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6thg RCSB], [https://www.ebi.ac.uk/pdbsum/6thg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6thg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/EFNB1_HUMAN EFNB1_HUMAN]] Craniofrontonasal dysplasia. The disease is caused by mutations affecting the gene represented in this entry. | + | [[https://www.uniprot.org/uniprot/EFNB1_HUMAN EFNB1_HUMAN]] Craniofrontonasal dysplasia. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/EFNB1_HUMAN EFNB1_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 (PubMed:8070404, PubMed:7973638). Binding to Eph receptors residing on adjacent cells leads to contact-dependent bidirectional signaling into neighboring cells (PubMed:8070404, PubMed:7973638). Shows high affinity for the receptor tyrosine kinase EPHB1/ELK (PubMed:8070404, PubMed:7973638). Can also bind EPHB2 and EPHB3 (PubMed:8070404). Binds to, and induces collapse of, commissural axons/growth cones in vitro (By similarity). May play a role in constraining the orientation of longitudinally projecting axons (By similarity).[UniProtKB:P52795]<ref>PMID:7973638</ref> <ref>PMID:8070404</ref> | + | [[https://www.uniprot.org/uniprot/EFNB1_HUMAN EFNB1_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 (PubMed:8070404, PubMed:7973638). Binding to Eph receptors residing on adjacent cells leads to contact-dependent bidirectional signaling into neighboring cells (PubMed:8070404, PubMed:7973638). Shows high affinity for the receptor tyrosine kinase EPHB1/ELK (PubMed:8070404, PubMed:7973638). Can also bind EPHB2 and EPHB3 (PubMed:8070404). Binds to, and induces collapse of, commissural axons/growth cones in vitro (By similarity). May play a role in constraining the orientation of longitudinally projecting axons (By similarity).[UniProtKB:P52795]<ref>PMID:7973638</ref> <ref>PMID:8070404</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 22: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6thg" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6thg" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ephrin|Ephrin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Disease
[EFNB1_HUMAN] Craniofrontonasal dysplasia. The disease is caused by mutations affecting the gene represented in this entry.
Function
[EFNB1_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 (PubMed:8070404, PubMed:7973638). Binding to Eph receptors residing on adjacent cells leads to contact-dependent bidirectional signaling into neighboring cells (PubMed:8070404, PubMed:7973638). Shows high affinity for the receptor tyrosine kinase EPHB1/ELK (PubMed:8070404, PubMed:7973638). Can also bind EPHB2 and EPHB3 (PubMed:8070404). Binds to, and induces collapse of, commissural axons/growth cones in vitro (By similarity). May play a role in constraining the orientation of longitudinally projecting axons (By similarity).[UniProtKB:P52795][1] [2]
Publication Abstract from PubMed
The emergent zoonotic henipaviruses, Hendra, and Nipah are responsible for frequent and fatal disease outbreaks in domestic animals and humans. Specificity of henipavirus attachment glycoproteins (G) for highly species-conserved ephrin ligands underpins their broad host range and is associated with systemic and neurological disease pathologies. Here, we demonstrate that Cedar virus (CedV)-a related henipavirus that is ostensibly nonpathogenic-possesses an idiosyncratic entry receptor repertoire that includes the common henipaviral receptor, ephrin-B2, but, distinct from pathogenic henipaviruses, does not include ephrin-B3. Uniquely among known henipaviruses, CedV can use ephrin-B1 for cellular entry. Structural analyses of CedV-G reveal a key region of molecular specificity that directs ephrin-B1 utilization, while preserving a universal mode of ephrin-B2 recognition. The structural and functional insights presented uncover diversity within the known henipavirus receptor repertoire and suggest that only modest structural changes may be required to modulate receptor specificities within this group of lethal human pathogens.
A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus.,Pryce R, Azarm K, Rissanen I, Harlos K, Bowden TA, Lee B Life Sci Alliance. 2019 Dec 20;3(1). pii: 3/1/e201900578. doi:, 10.26508/lsa.201900578. Print 2020 Jan. PMID:31862858[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Davis S, Gale NW, Aldrich TH, Maisonpierre PC, Lhotak V, Pawson T, Goldfarb M, Yancopoulos GD. Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity. Science. 1994 Nov 4;266(5186):816-9. doi: 10.1126/science.7973638. PMID:7973638 doi:http://dx.doi.org/10.1126/science.7973638
- ↑ Beckmann MP, Cerretti DP, Baum P, Vanden Bos T, James L, Farrah T, Kozlosky C, Hollingsworth T, Shilling H, Maraskovsky E, et al.. Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors. EMBO J. 1994 Aug 15;13(16):3757-62. PMID:8070404
- ↑ Pryce R, Azarm K, Rissanen I, Harlos K, Bowden TA, Lee B. A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus. Life Sci Alliance. 2019 Dec 20;3(1). pii: 3/1/e201900578. doi:, 10.26508/lsa.201900578. Print 2020 Jan. PMID:31862858 doi:http://dx.doi.org/10.26508/lsa.201900578
|
