ArticleEMBO reports2009
Ligand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex.
Article in EMBO reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed.
- Molecular Determinants of Receptor-Specific Membrane Interactions in EphA1 and EphA2 from Coarse-Grained Simulations.Journal of chemical information and modeling · 2026Article
- Frequent EPHA2 receptor mutations in cholangiocarcinoma disrupt receptor forward signaling supporting a tumor suppressor role.Biochimica et biophysica acta. Molecular cell research · 2026Article
- The Interaction between the Tyrosine Kinase Receptor EphA2 and RNF5: Structural Insights from anComputational and structural biotechnology journal · 2026Article
- EphA2 and Ephrin-A1 Utilize the Same Interface for BothbioRxiv : the preprint server for biology · 2025Article
- NMR resonance assignment of a ligand-binding domain of ephrin receptor A2.Biomolecular NMR assignments · 2025Article
- Synthetic antibodies targeting EphA2 induce diverse signaling-competent clusters with differential activation.Protein science : a publication of the Protein Society · 2025Article
- Targeting the EphA2 pathway: could it be the way for bone sarcomas?Cell communication and signaling : CCS · 2024Review
- Dioxinodehydroeckol: A Potential Neuroprotective Marine Compound Identified by In Silico Screening for the Treatment and Management of Multiple Brain Disorders.Molecular biotechnology · 2024Article
- Targeting EphA2: a promising strategy to overcome chemoresistance and drug resistance in cancer.Journal of molecular medicine (Berlin, Germany) · 2024Review
- Molecular Determinants of EphA2 and EphB2 Antagonism Enable the Design of Ligands with Improved Selectivity.Journal of chemical information and modeling · 2023Article
- Overexpression of hepatocyte EphA2 enhances liver-stage infection by Plasmodium vivax.Scientific reports · 2022Article
- Role of EFNA1 SNP (rs12904) in Tumorigenesis and Metastasis of Colorectal Cancer: A Bioinformatic Analysis and HRM SNP Genotyping Verification.Asian Pacific journal of cancer prevention : APJCP · 2022Article
- Contrastive learning on protein embeddings enlightens midnight zone.NAR genomics and bioinformatics · 2022Article
- Review
- Protein-Protein Interaction Inhibitors Targeting the Eph-Ephrin System with a Focus on Amino Acid Conjugates of Bile Acids.Pharmaceuticals (Basel, Switzerland) · 2022Review
- The Ephb2 Receptor Uses Homotypic, Head-to-Tail Interactions within Its Ectodomain as an Autoinhibitory Control Mechanism.International journal of molecular sciences · 2021Article
- EphA2 signaling within integrin adhesions regulates fibrillar adhesion elongation and fibronectin deposition.Matrix biology : journal of the International Society for Matrix Biology · 2021Article
- Human herpesvirus 8 molecular mimicry of ephrin ligands facilitates cell entry and triggers EphA2 signaling.PLoS biology · 2021Article
- Effects of EFNA1 on cell phenotype and prognosis of esophageal carcinoma.World journal of surgical oncology · 2021Article
- The EphB6 Receptor: Kinase-Dead but Very Much Alive.International journal of molecular sciences · 2021Review
18 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors.
Funding
Abstract
Ephrin (Eph) receptor tyrosine kinases fall into two subclasses (A and B) according to preferences for their ephrin ligands. All published structural studies of Eph receptor/ephrin complexes involve B-class receptors. Here, we present the crystal structures of an A-class complex between EphA2 and ephrin-A1 and of unbound EphA2. Although these structures are similar overall to their B-class counterparts, they reveal important differences that define subclass specificity. The structures suggest that the A-class Eph receptor/ephrin interactions involve smaller rearrangements in the interacting partners, better described by a 'lock-and-key'-type binding mechanism, in contrast to the 'induced fit' mechanism defining the B-class molecules. This model is supported by structure-based mutagenesis and by differential requirements for ligand oligomerization by the two subclasses in cell-based Eph receptor activation assays. Finally, the structure of the unligated receptor reveals a homodimer assembly that might represent EphA2-specific homotypic cell adhesion interactions.
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