NDLI: Insights into Eph receptor tyrosine kinase activation from crystal structures of the EphA4 ectodomain and its complex with ephrin-A5

Content Provider	PubMed Central
Author	Xu, Kai Dorothea, Tzvetkova-robev Xu, Yan Yehuda, Goldgur Chan, Yee-peng Himanen, Juha P. Nikolov, Dimitar B.
Abstract	Our paper describes the high-resolution structures of the complete EphA4 receptor tyrosine kinase ectodomain and its complex with ephrin-A5. These structures reveal for the first time how ephrin binding promotes Eph conformational changes allowing for the formation of ordered signaling clusters at the sites of cell–cell contact. In addition, the structural data, combined with structure-based mutagenesis and cell-based assays, reveal a previously undescribed receptor–receptor interaction between the EphA4 ligand-binding and membrane-proximal fibronectin domains, which is functionally important for efficient Eph activation. Based on the data we suggest a mechanism for Eph preclustering and recruitment of unliganded Eph into existing Eph/ephrin signaling clusters.
Related Links	http://dx.doi.org/10.1073/pnas.1311000110
Ending Page	14639
Page Count	6
Starting Page	14634
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	36
Volume Number	110
Language	English
Publisher	National Academy of Sciences
Publisher Date	2013-09-03
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Insights into Eph receptor tyrosine kinase activation from crystal structures of the EphA4 ectodomain and its complex with ephrin-A5