Crystal structure of an Eph receptor-ephrin complex.

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.
Mesh Terms:
Amino Acid Sequence, Animals, Crystallography, X-Ray, Dimerization, Ephrin-B2, Escherichia coli, Ligands, Macromolecular Substances, Membrane Proteins, Mice, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Receptor Protein-Tyrosine Kinases, Receptor, EphB2, Recombinant Proteins, Sequence Alignment
Nature
Date: Jan. 10, 2002
Download Curated Data For This Publication
9505
Switch View:
  • Interactions 1