ArticlePloS one2014
Crystal structure of arginine methyltransferase 6 from Trypanosoma brucei.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Stability-Driven Pose Prediction and Ligand Design via Contact Persistence Analysis from Molecular Dynamics Simulations.Computational and structural biotechnology journal · 2026Article
- Protein arginine methyltransferases in protozoan parasites: a new path for antiparasitic chemotherapy?Microbial cell (Graz, Austria) · 2026Article
- A type II protein arginine methyltransferase regulates merozoite invasion in Plasmodium falciparum.Communications biology · 2023Article
- Protein arginine methyltransferases in protozoan parasites.Parasitology · 2022Review
- Structure, Activity and Function of the Protein Arginine Methyltransferase 6.Life (Basel, Switzerland) · 2021Review
- Arginine Methyltransferases as Regulators of RNA-Binding Protein Activities in Pathogenic Kinetoplastids.Frontiers in molecular biosciences · 2021Review
- Structural Basis of Protein Arginine Methyltransferase Activation by a Catalytically Dead Homolog (Prozyme).Journal of molecular biology · 2020Article
- Protein arginine methyltransferases: insights into the enzyme structure and mechanism at the atomic level.Cellular and molecular life sciences : CMLS · 2019Review
- The Major Protein Arginine Methyltransferase inThe Journal of biological chemistry · 2017Article
- Structural basis of arginine asymmetrical dimethylation by PRMT6.The Biochemical journal · 2016Article
- Epigenetics in Schistosomes: What We Know and What We Need Know.Frontiers in cellular and infection microbiology · 2016Review
- Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity.Biochemistry · 2015Article
- The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond.Cellular and molecular life sciences : CMLS · 2015Review
- Computational Study of Symmetric Methylation on Histone Arginine Catalyzed by Protein Arginine Methyltransferase PRMT5 through QM/MM MD and Free Energy Simulations.Molecules (Basel, Switzerland) · 2015Article
- Exploration of cyanine compounds as selective inhibitors of protein arginine methyltransferases: synthesis and biological evaluation.Journal of medicinal chemistry · 2015Article
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Authors and funding
15 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arginine methylation plays vital roles in the cellular functions of the protozoan Trypanosoma brucei. The T. brucei arginine methyltransferase 6 (TbPRMT6) is a type I arginine methyltransferase homologous to human PRMT6. In this study, we report the crystal structures of apo-TbPRMT6 and its complex with the reaction product S-adenosyl-homocysteine (SAH). The structure of apo-TbPRMT6 displays several features that are different from those of type I PRMTs that were structurally characterized previously, including four stretches of insertion, the absence of strand β15, and a distinct dimerization arm. The comparison of the apo-TbPRMT6 and SAH-TbPRMT6 structures revealed the fine rearrangements in the active site upon SAH binding. The isothermal titration calorimetry results demonstrated that SAH binding greatly increases the affinity of TbPRMT6 to a substrate peptide derived from bovine histone H4. The western blotting and mass spectrometry results revealed that TbPRMT6 methylates bovine histone H4 tail at arginine 3 but cannot methylate several T. brucei histone tails. In summary, our results highlight the structural differences between TbPRMT6 and other type I PRMTs and reveal that the active site rearrangement upon SAH binding is important for the substrate binding of TbPRMT6.
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