Ephs and ephrins close ranks.
The past decade has seen remarkable advances in identification of the proteins regulating axon guidance and synapse formation. Understanding the structural and molecular basis of their signaling properties is now the task at hand. The recently characterized crystal structure of the complex formed between the ligand-binding domain of EphB2 and the ectodomain of its binding partner ephrin-B2 provides an insight into the recognition and signal transduction mechanisms of this large multifunctional family of surface receptors. This heterotetrameric complex reveals a cyclic arrangement of subunits not previously seen in any receptor-ligand structure, and provides a basis for class specificity of binding.
Cutforth
Tyler
T
Center for Neurobiology and Behavior, Columbia University, 701 W. 168 St, New York, NY 10032, USA.
Harrison
Celia J
CJ
D000818:Animals; D002450:Cell Communication / Q000502:physiology*; D002454:Cell Differentiation / Q000502:physiology*; D002490:Central Nervous System / Q000196:embryology* / Q000378:metabolism*; D002630:Chemotactic Factors / Q000378:metabolism*; D036388:Ephrin-B2; D020439:Growth Cones / Q000378:metabolism*; D006801:Humans; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000378:metabolism*; D015394:Molecular Structure; D011485:Protein Binding / Q000502:physiology; D020794:Receptor Protein-Tyrosine Kinases / Q000378:metabolism*; D036183:Receptor, EphB2; D015398:Signal Transduction / Q000502:physiology
D002630:Chemotactic Factors; D036388:Ephrin-B2; D046911:Macromolecular Substances; D008565:Membrane Proteins; D020794:Receptor Protein-Tyrosine Kinases; D036183:Receptor, EphB2