Crystal structure of an Eph receptor-ephrin complex

J. P. Himanen, K. R. Rajashankar, M. Lackmann, C. A. Cowan, M. Henkemeyer, D. B. Nikolov

Research output: Contribution to journalArticlepeer-review

269 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)933-938
Number of pages6
Issue number6866
StatePublished - Dec 20 2001

ASJC Scopus subject areas

  • General


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