ArticleBiochemical and biophysical research communications2010
Crystal structure of the ligand-binding domain of the promiscuous EphA4 receptor reveals two distinct conformations.
Article in Biochemical and biophysical research communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Database-Driven Identification of Structurally Similar Protein-Protein Interfaces.Journal of chemical information and modeling · 2024Article
- Spatial-temporal comparison of Eph/Ephrin gene expression in ocular lenses from aging and knockout mice.Frontiers in ophthalmology · 2024Article
- A computational and laboratory approach for the investigation of interactions of peptide conjugated natural terpenes with EpHA2 receptor.Journal of molecular modeling · 2023Article
- Structure of the EphB6 receptor ectodomain.PloS one · 2021Article
- Glycoengineering of EphA4 Fc leads to a unique, long-acting and broad spectrum, Eph receptor therapeutic antagonist.Scientific reports · 2017Article
- Identification and characterization of Nanobodies targeting the EphA4 receptor.The Journal of biological chemistry · 2017Article
- Potent and Selective EphA4 Agonists for the Treatment of ALS.Cell chemical biology · 2017Article
- Gene Expression Profiling of Muscle Stem Cells Identifies Novel Regulators of Postnatal Myogenesis.Frontiers in cell and developmental biology · 2016Article
- Development and structural analysis of a nanomolar cyclic peptide antagonist for the EphA4 receptor.ACS chemical biology · 2014Article
- Promiscuous and specific recognition among ephrins and Eph receptors.Biochimica et biophysica acta · 2014Article
- Blockade of EphA4 signaling ameliorates hippocampal synaptic dysfunctions in mouse models of Alzheimer's disease.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Regulation of signaling interactions and receptor endocytosis in growing blood vessels.Cell adhesion & migration · 2014Review
- Insights into Eph receptor tyrosine kinase activation from crystal structures of the EphA4 ectodomain and its complex with ephrin-A5.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.The Journal of biological chemistry · 2013Article
- Article
- Global evaluation of Eph receptors and ephrins in lung adenocarcinomas identifies EphA4 as an inhibitor of cell migration and invasion.Molecular cancer therapeutics · 2012Article
- Coordinated Eph-ephrin signaling guides migration and axon targeting in the avian auditory system.Neural development · 2012Article
- EphrinA1 is released in three forms from cancer cells by matrix metalloproteases.Molecular and cellular biology · 2012Article
- Distinctive binding of three antagonistic peptides to the ephrin-binding pocket of the EphA4 receptor.The Biochemical journal · 2012Article
- Ephs and ephrins in cancer: ephrin-A1 signalling.Seminars in cell & developmental biology · 2012Review
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Authors and funding
6 authors.
Funding
Abstract
Eph receptors and their ephrin ligands are important mediators of cell-cell communication. They are divided in two subclasses based on their affinities for each other and on sequence conservation. Receptor-ligand binding within each subclass is fairly promiscuous, while binding cross the subclasses happens rarely. EphA4 is an exception to this general rule, since it has long been known to bind both A- and B-class ephrin ligands but the reason for this exceptional behavior has not been worked out at molecular level. Recent structural and biochemical studies on EphA4 ligand-binding domain alone and in complex with its ligands have addressed this question. However, the published structures of EphA4/ephrin complexes differ considerably from each other and strikingly different explanations for the exceptional promiscuity of EphA4 were proposed. To address these contradictory findings, we have determined a crystal structure of the EphA4 ligand-binding domain at 2.3A resolution and show that the receptor has an unprecedented ability to exist in two very different, well-ordered conformations even in the unbound state. Our results suggest that the ligand promiscuity of the Ephs is directly correlated with the structural flexibility of the ligand-binding surface of the receptor.
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