Crystal structure of an Eph receptor–ephrin complex

Juha-Pekka Himanen, Kanagalaghatta R. Rajashankar, Martin Lackmann, Chad A. Cowan, Mark Henkemeyer and Dimitar B. Nikolov ()
Additional contact information
Juha-Pekka Himanen: Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center
Kanagalaghatta R. Rajashankar: Brookhaven National Laboratory
Martin Lackmann: Ludwig Institute for Cancer Research, Royal Melbourne Hospital
Chad A. Cowan: Center for Developmental Biology and Kent Waldrep Foundation Center for Basic Research on Nerve Growth and Regeneration, University of Texas Southwestern Medical Center
Mark Henkemeyer: Center for Developmental Biology and Kent Waldrep Foundation Center for Basic Research on Nerve Growth and Regeneration, University of Texas Southwestern Medical Center
Dimitar B. Nikolov: Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center

Nature, 2001, vol. 414, issue 6866, 933-938

Abstract: 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.

Date: 2001
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/414933a Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:414:y:2001:i:6866:d:10.1038_414933a

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/414933a

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().