1kgy
From Proteopedia
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'''Crystal Structure of the EphB2-ephrinB2 complex''' | '''Crystal Structure of the EphB2-ephrinB2 complex''' | ||
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[[Category: Nikolov, D B.]] | [[Category: Nikolov, D B.]] | ||
[[Category: Rajashankar, K R.]] | [[Category: Rajashankar, K R.]] | ||
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Revision as of 19:44, 2 May 2008
Crystal Structure of the EphB2-ephrinB2 complex
Overview
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.
About this Structure
1KGY is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of an Eph receptor-ephrin complex., Himanen JP, Rajashankar KR, Lackmann M, Cowan CA, Henkemeyer M, Nikolov DB, Nature. 2001 Dec 20-27;414(6866):933-8. PMID:11780069 Page seeded by OCA on Fri May 2 22:44:03 2008
