| First Author | Himanen JP | Year | 2001 |
| Journal | Nature | Volume | 414 |
| Issue | 6866 | Pages | 933-8 |
| PubMed ID | 11780069 | Mgi Jnum | J:73356 |
| Mgi Id | MGI:2155002 | Doi | 10.1038/414933a |
| Citation | Himanen JP, et al. (2001) Crystal structure of an Eph receptor-ephrin complex. Nature 414(6866):933-8 |
| abstractText | The Eph family of receptor tyrosine kinases and their membrane-anchored ephrin ligands are important in regulating cell-cell interactions as they initiate a unique bidirectional signal transduction cascade whereby information is communicated into both the Eph-expressing and the ephrin-expressing cells. Initially identified as regulators of axon pathfinding and neuronal cell migration, Ephs and ephrins are now known to have roles in many other cell-cell interactions, including those of vascular endothelial cells and specialized epithelia. Here we report the crystal structure of the complex formed between EphB2 and ephrin-B2, determined at 2.7 A resolution. Each Eph receptor binds an ephrin ligand through an expansive dimerization interface dominated by the insertion of an extended ephrin loop into a channel at the surface of the receptor. Two Eph-Ephrin dimers then join to form a tetramer, in which each ligand interacts with two receptors and each receptor interacts with two ligands. The Eph and ephrin molecules are precisely positioned and orientated in these complexes, promoting higher-order clustering and the initiation of bidirectional signalling. |
