1KGY

Crystal Structure of the EphB2-ephrinB2 complex

Summary for 1KGY

• Entry DOI: 10.2210/pdb1kgy/pdb
• Descriptor: EPHRIN TYPE-B RECEPTOR 2, EPHRIN-B2 (2 entities in total)
• Functional Keywords: developmental protein, transferase-transferase receptor complex, transferase/transferase receptor
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cell membrane; Single-pass type I membrane protein: P54763; Membrane; Single-pass type I membrane protein: P52800
• Total number of polymer chains: 8
• Total formula weight: 146289.98

Authors

Himanen, J.P.,Rajashankar, K.R.,Lackmann, M.,Cowan, C.A.,Henkemeyer, M.,Nikolov, D.B. (deposition date: 2001-11-28, release date: 2002-05-28, Last modification date: 2024-10-30)

Primary citation

Himanen, J.P.,Rajashankar, K.R.,Lackmann, M.,Cowan, C.A.,Henkemeyer, M.,Nikolov, D.B.
Crystal structure of an Eph receptor-ephrin complex.
Nature, 414:933-938, 2001

PubMed 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 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.

PubMed: 11780069
DOI: 10.1038/414933a

Experimental method

X-RAY DIFFRACTION (2.7 Å)