ArticlePloS one2015
Distinctive Structure of the EphA3/Ephrin-A5 Complex Reveals a Dual Mode of Eph Receptor Interaction for Ephrin-A5.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Indolium 1 Exerts Activity against Vemurafenib-Resistant Melanoma In Vivo.Antioxidants (Basel, Switzerland) · 2022Article
- The Hippo effector YAP1/TEAD1 regulates EPHA3 expression to control cell contact and motility.Scientific reports · 2022Article
- NMR-Guided Design of Potent and Selective EphA4 Agonistic Ligands.Journal of medicinal chemistry · 2021Article
- CCR10+ epithelial cells from idiopathic pulmonary fibrosis lungs drive remodeling.JCI insight · 2018Article
- EphA2 and ephrin-A5 are not a receptor-ligand pair in the ocular lens.Experimental eye research · 2017Article
- Potent and Selective EphA4 Agonists for the Treatment of ALS.Cell chemical biology · 2017Article
- Novel Nine-Exon AR Transcripts (Exon 1/Exon 1b/Exons 2-8) in Normal and Cancerous Breast and Prostate Cells.International journal of molecular sciences · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The Eph receptor tyrosine kinase/ephrin ligand system regulates a wide spectrum of physiological processes, while its dysregulation has been implicated in cancer progression. The human EphA3 receptor is widely upregulated in the tumor microenvironment and is highly expressed in some types of cancer cells. Furthermore, EphA3 is among the most highly mutated genes in lung cancer and it is also frequently mutated in other cancers. We report the structure of the ligand-binding domain of the EphA3 receptor in complex with its preferred ligand, ephrin-A5. The structure of the complex reveals a pronounced tilt of the ephrin-A5 ligand compared to its orientation when bound to the EphA2 and EphB2 receptors and similar to its orientation when bound to EphA4. This tilt brings an additional area of ephrin-A5 into contact with regions of EphA3 outside the ephrin-binding pocket thereby enlarging the size of the interface, which is consistent with the high binding affinity of ephrin-A5 for EphA3. This large variation in the tilt of ephrin-A5 bound to different Eph receptors has not been previously observed for other ephrins.
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Registered trials
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