6thg
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Cedar Virus attachment glycoprotein (G) in complex with human ephrin-B1== | |
- | + | <StructureSection load='6thg' size='340' side='right'caption='[[6thg]], [[Resolution|resolution]] 4.07Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[6thg]] is a 10 chain structure. 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> | |
- | + | </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> | |
- | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6thb|6thb]]</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> | ||
+ | </table> | ||
+ | == 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. | ||
+ | == 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> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Bowden, T]] | ||
+ | [[Category: Harlos, K]] | ||
+ | [[Category: Pryce, R]] | ||
+ | [[Category: Rissanen, I]] | ||
+ | [[Category: Attachment glycoprotein]] | ||
+ | [[Category: Beta-propeller]] | ||
+ | [[Category: Complex]] | ||
+ | [[Category: Ephrin-b1]] | ||
+ | [[Category: Viral protein]] |
Revision as of 07:57, 18 December 2019
Cedar Virus attachment glycoprotein (G) in complex with human ephrin-B1
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