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| {{STRUCTURE_1shw| PDB=1shw | SCENE= }} | | {{STRUCTURE_1shw| PDB=1shw | SCENE= }} |
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| '''EphB2 / EphrinA5 Complex Structure'''
| | ===EphB2 / EphrinA5 Complex Structure=== |
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| ==Overview==
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| The interactions between Eph receptor tyrosine kinases and their ephrin ligands regulate cell migration and axon pathfinding. The EphA receptors are generally thought to become activated by ephrin-A ligands, whereas the EphB receptors interact with ephrin-B ligands. Here we show that two of the most widely studied of these molecules, EphB2 and ephrin-A5, which have never been described to interact with each other, do in fact bind one another with high affinity. Exposure of EphB2-expressing cells to ephrin-A5 leads to receptor clustering, autophosphorylation and initiation of downstream signaling. Ephrin-A5 induces EphB2-mediated growth cone collapse and neurite retraction in a model system. We further show, using X-ray crystallography, that the ephrin-A5-EphB2 complex is a heterodimer and is architecturally distinct from the tetrameric EphB2-ephrin-B2 structure. The structural data reveal the molecular basis for EphB2-ephrin-A5 signaling and provide a framework for understanding the complexities of functional interactions and crosstalk between A- and B-subclass Eph receptors and ephrins. | | The line below this paragraph, {{ABSTRACT_PUBMED_15107857}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15107857 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15107857}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Ephrin signaling]] | | [[Category: Ephrin signaling]] |
| [[Category: Receptor tyrosine kinase]] | | [[Category: Receptor tyrosine kinase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:43:33 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:18:31 2008'' |
