Crystal structure of an Eph receptor-ephrin complex Journal Article
| Authors: | Himanen, J. P.; Rajashankar, K. R.; Lackmann, M.; Cowan, C. A.; Henkemeyer, M.; Nikolov, D. B. |
| Article Title: | Crystal structure of an Eph receptor-ephrin complex |
| Abstract: | 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 epithelia1,2 Here we report the crystal structure of the complex formed between EphB2 and ephrin-B2, determined at 2.7 Å 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. |
| Keywords: | signal transduction; protein conformation; animals; mice; complex formation; protein binding; membrane proteins; endothelium cell; amino acid sequence; molecular sequence data; vascular endothelium; sequence alignment; nerve fiber; escherichia coli; recombinant proteins; tyrosine kinase receptor; ligand; cell migration; ligands; crystal structure; models, molecular; dimerization; crystallography, x-ray; receptor protein-tyrosine kinases; cell interaction; receptor, ephb2; enzymes; receptor binding; macromolecular substances; ephrin; cells; molecules; dimer; biological membranes; ephrin receptor; dimers; ephrin-b2; priority journal; article; insertion sequences |
| Journal Title: | Nature |
| Volume: | 414 |
| Issue: | 6866 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 2001-12-20 |
| Start Page: | 933 |
| End Page: | 938 |
| Language: | English |
| DOI: | 10.1038/414933a |
| PUBMED: | 11780069 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 21 May 2015 -- Source: Scopus |
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