1shw
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(New page: 200px<br /><applet load="1shw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1shw, resolution 2.2Å" /> '''EphB2 / EphrinA5 Comp...)
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Revision as of 00:16, 21 November 2007
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EphB2 / EphrinA5 Complex Structure
Overview
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.
About this Structure
1SHW is a Protein complex structure of sequences from Mus musculus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Repelling class discrimination: ephrin-A5 binds to and activates EphB2 receptor signaling., Himanen JP, Chumley MJ, Lackmann M, Li C, Barton WA, Jeffrey PD, Vearing C, Geleick D, Feldheim DA, Boyd AW, Henkemeyer M, Nikolov DB, Nat Neurosci. 2004 May;7(5):501-9. Epub 2004 Apr 25. PMID:15107857
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