ArticleThe Journal of biological chemistry2009
Structural insights into parasite eIF4E binding specificity for m7G and m2,2,7G mRNA caps.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 41 citations in OpenAlex.
- PDCD4: A Double-Edged Sword in Neurological Diseases.Molecular neurobiology · 2026Review
- mRNA based vaccines and therapeutics for parasitic infections: a comprehensive review.Journal of nanobiotechnology · 2025Review
- Establishment of minigenomes for infectious bursal disease virus.Veterinary research · 2024Article
- Emerging influence of RNA post-transcriptional modifications in the synovial homeostasis of rheumatoid arthritis.Frontiers in immunology · 2024Review
- The translation initiation factor EIF4E5 from Leishmania: crystal structure and interacting partners.RNA biology · 2021Article
- Structural Insights into the Interaction of Clinically Relevant Phosphorothioate mRNA Cap Analogs with Translation Initiation Factor 4E Reveal Stabilization via Electrostatic Thio-Effect.ACS chemical biology · 2021Article
- Computational study on the allosteric mechanism ofComputational and structural biotechnology journal · 2021Article
- Loss of the RNA trimethylguanosine cap is compatible with nuclear accumulation of spliceosomal snRNAs but not pre-mRNA splicing or snRNA processing during animal development.PLoS genetics · 2020Article
- Functional characterization of the translation initiation factor eIF4E of Echinococcus granulosus.Parasitology research · 2019Article
- Crystal structure of the Trypanosoma cruzi EIF4E5 translation factor homologue in complex with mRNA cap-4.Nucleic acids research · 2019Article
- Synthesis of 7-benzylguanosine cap-analogue conjugates for eIF4E targeted degradation.European journal of medicinal chemistry · 2019Article
- Predictions of novel Schistosoma mansoni - human protein interactions consistent with experimental data.Scientific reports · 2018Article
- A general method for rapid and cost-efficient large-scale production of 5' capped RNA.RNA (New York, N.Y.) · 2016Article
- Characterization of the Raptor/4E-BP1 interaction by chemical cross-linking coupled with mass spectrometry analysis.The Journal of biological chemistry · 2014Article
- The soy isoflavone equol may increase cancer malignancy via up-regulation of eukaryotic protein synthesis initiation factor eIF4G.The Journal of biological chemistry · 2012Article
- Synthesis of N²-modified 7-methylguanosine 5'-monophosphates as nematode translation inhibitors.Bioorganic & medicinal chemistry · 2012Article
- Synthesis of ¹³C- and ¹⁴C-labeled dinucleotide mRNA cap analogues for structural and biochemical studies.Bioorganic & medicinal chemistry letters · 2012Article
- Structural basis for nematode eIF4E binding an m(2,2,7)G-Cap and its implications for translation initiation.Nucleic acids research · 2011Article
- Dynamical insight into Caenorhabditis elegans eIF4E recognition specificity for mono-and trimethylated structures of mRNA 5' cap.Journal of molecular modeling · 2011Article
- Structure-based mutational analysis of eIF4E in relation to sbm1 resistance to pea seed-borne mosaic virus in pea.PloS one · 2011Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
The eukaryotic translation initiation factor eIF4E recognizes the mRNA cap, a key step in translation initiation. Here we have characterized eIF4E from the human parasite Schistosoma mansoni. Schistosome mRNAs have either the typical monomethylguanosine (m(7)G) or a trimethylguanosine (m(2,2,7)G) cap derived from spliced leader trans-splicing. Quantitative fluorescence titration analyses demonstrated that schistosome eIF4E has similar binding specificity for both caps. We present the first crystal structure of an eIF4E with similar binding specificity for m(7)G and m(2,2,7)G caps. The eIF4E.m(7)GpppG structure demonstrates that the schistosome protein binds monomethyl cap in a manner similar to that of single specificity eIF4Es and exhibits a structure similar to other known eIF4Es. The structure suggests an alternate orientation of a conserved, key Glu-90 in the cap-binding pocket that may contribute to dual binding specificity and a position for mRNA bound to eIF4E consistent with biochemical data. Comparison of NMR chemical shift perturbations in schistosome eIF4E on binding m(7)GpppG and m(2,2,7)GpppG identified key differences between the two complexes. Isothermal titration calorimetry demonstrated significant thermodynamics differences for the binding process with the two caps (m(7)G versus m(2,2,7)G). Overall the NMR and isothermal titration calorimetry data suggest the importance of intrinsic conformational flexibility in the schistosome eIF4E that enables binding to m(2,2,7)G cap.
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