1SHW
EphB2 / EphrinA5 Complex Structure
Summary for 1SHW
| Entry DOI | 10.2210/pdb1shw/pdb |
| Related | 1NUK 1SHX |
| Related PRD ID | PRD_900017 |
| Descriptor | Ephrin-A5, Ephrin type-B receptor 2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | receptor tyrosine kinase, ephrin signaling, hormone-growth factor-receptor complex, hormone/growth factor/receptor |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 2 |
| Total formula weight | 37897.90 |
| Authors | Himanen, J.P.,Chumley, M.J.,Lackmann, M.,Li, C.,Barton, W.A.,Jeffrey, P.D.,Vearing, C.,Geleick, D.,Feldheim, D.A.,Boyd, A.W. (deposition date: 2004-02-26, release date: 2004-05-18, Last modification date: 2024-10-30) |
| Primary citation | Himanen, J.P.,Chumley, M.J.,Lackmann, M.,Li, C.,Barton, W.A.,Jeffrey, P.D.,Vearing, C.,Geleick, D.,Feldheim, D.A.,Boyd, A.W.,Henkemeyer, M.,Nikolov, D.B. Repelling class discrimination: ephrin-A5 binds to and activates EphB2 receptor signaling Nat.Neurosci., 7:501-509, 2004 Cited by PubMed Abstract: 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. PubMed: 15107857DOI: 10.1038/nn1237 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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