1shx

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[[Image:1shx.png|left|200px]]
 
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{{STRUCTURE_1shx| PDB=1shx | SCENE= }}
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==Ephrin A5 ligand structure==
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<StructureSection load='1shx' size='340' side='right'caption='[[1shx]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1shx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SHX FirstGlance]. <br>
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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]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=1shx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1shx OCA], [https://pdbe.org/1shx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1shx RCSB], [https://www.ebi.ac.uk/pdbsum/1shx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1shx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/EFNA5_MOUSE EFNA5_MOUSE] Cell surface GPI-bound 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. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion.<ref>PMID:9053851</ref> <ref>PMID:11089974</ref> <ref>PMID:17448994</ref> <ref>PMID:18948590</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sh/1shx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1shx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Eph receptor tyrosine kinases (Ephs) function as molecular relays that interact with cell surface-bound ephrin ligands to direct the position of migrating cells. Structural studies revealed that, through two distinct contact surfaces on opposite sites of each protein, Eph and ephrin binding domains assemble into symmetric, circular heterotetramers. However, Eph signal initiation requires the assembly of higher order oligomers, suggesting additional points of contact. By screening a random library of EphA3 binding-compromised ephrin-A5 mutants, we have now determined ephrin-A5 residues that are essential for the assembly of high affinity EphA3 signaling complexes. In addition to the two interfaces predicted from the crystal structure of the homologous EphB2.ephrin-B2 complex, we identified a cluster of 10 residues on the ephrin-A5 E alpha-helix, the E-F loop, the underlying H beta-strand, as well as the nearby B-C loop, which define a distinct third surface required for oligomerization and activation of EphA3 signaling. Together with a corresponding third surface region identified recently outside of the minimal ephrin binding domain of EphA3, our findings provide experimental evidence for the essential contribution of three distinct protein-interaction interfaces to assemble functional EphA3 signaling complexes.
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===Ephrin A5 ligand structure===
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Three distinct molecular surfaces in ephrin-A5 are essential for a functional interaction with EphA3.,Day B, To C, Himanen JP, Smith FM, Nikolov DB, Boyd AW, Lackmann M J Biol Chem. 2005 Jul 15;280(28):26526-32. Epub 2005 May 18. PMID:15901737<ref>PMID:15901737</ref>
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{{ABSTRACT_PUBMED_15901737}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 1shx" style="background-color:#fffaf0;"></div>
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[[1shx]] is a 2 chain structure of [[Ephrin receptor]] with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHX OCA].
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==See Also==
==See Also==
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*[[Ephrin receptor|Ephrin receptor]]
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*[[Ephrin|Ephrin]]
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*[[Ephrin receptor 3D structures|Ephrin receptor 3D structures]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:015901737</ref><ref group="xtra">PMID:015114347</ref><references group="xtra"/>
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Barton, W A.]]
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[[Category: Barton WA]]
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[[Category: Himanen, J P.]]
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[[Category: Himanen JP]]
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[[Category: Jeffrey, P D.]]
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[[Category: Jeffrey PD]]
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[[Category: Nikolov, D B.]]
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[[Category: Nikolov DB]]
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[[Category: Ephrin signaling]]
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[[Category: Hormone-growth factor complex]]
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Ephrin A5 ligand structure

PDB ID 1shx

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