ArticleNucleic acids research2011
Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 65 citations in OpenAlex.
- ThebioRxiv : the preprint server for biology · 2026Article
- Epigenetic Functions of SMYD5 and Its Role in Development, Cancer and Other Cellular Processes.International journal of molecular sciences · 2026Review
- Role of SMYD2 in gastrointestinal cancer progression (Review).Oncology letters · 2025Review
- Zinc finger myeloid Nervy DEAF-1 type (ZMYND) domain containing proteins exert molecular interactions to implicate in carcinogenesis.Discover oncology · 2022Review
- The Role of the TSK/TONSL-H3.1 Pathway in Maintaining Genome Stability in Multicellular Eukaryotes.International journal of molecular sciences · 2022Review
- Unique SMYD5 Structure Revealed by AlphaFold Correlates with Its Functional Divergence.Biomolecules · 2022Article
- Lysine methyltransferase inhibitors: where we are now.RSC chemical biology · 2022Review
- The Methyltransferase Smyd1 Mediates LPS-Triggered Up-Regulation of IL-6 in Endothelial Cells.Cells · 2021Article
- Mechanism of the Conformational Change of the Protein Methyltransferase SMYD3: A Molecular Dynamics Simulation Study.International journal of molecular sciences · 2021Article
- Dynamic methylation of histone H3K18 in differentiating Theileria parasites.Nature communications · 2021Article
- Discovery of an Allosteric Ligand Binding Site in SMYD3 Lysine Methyltransferase.Chembiochem : a European journal of chemical biology · 2021Article
- Article
- LncRNA LTSCCAT promotes tongue squamous cell carcinoma metastasis via targeting the miR-103a-2-5p/SMYD3/TWIST1 axis.Cell death & disease · 2021Article
- Controlled "off-on" fluorescent probe for the specific detection of hyperhomocysteinemia.RSC advances · 2021Article
- Targeting Epigenetic Mechanisms in Vascular Aging.Frontiers in cardiovascular medicine · 2021Review
- The function of histone lysine methylation related SET domain group proteins in plants.Protein science : a publication of the Protein Society · 2020Review
- Review
- Function of the MYND Domain and C-Terminal Region in Regulating the Subcellular Localization and Catalytic Activity of the SMYD Family Lysine Methyltransferase Set5.Molecular and cellular biology · 2020Article
- Host factor SMYD3 is recruited by Ebola virus nucleoprotein to facilitate viral mRNA transcription.Emerging microbes & infections · 2019Article
- The Smyd Family of Methyltransferases: Role in Cardiac and Skeletal Muscle Physiology and Pathology.Current opinion in physiology · 2018Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The SET- and MYND-domain containing (Smyd) proteins constitute a special subfamily of the SET-containing lysine methyltransferases. Here we present the structure of full-length human Smyd3 in complex with S-adenosyl-L-homocysteine at 2.8 Å resolution. Smyd3 affords the first example that other region(s) besides the SET domain and its flanking regions participate in the formation of the active site. Structural analysis shows that the previously uncharacterized C-terminal domain of Smyd3 contains a tetratrico-peptide repeat (TPR) domain which together with the SET and post-SET domains forms a deep, narrow substrate binding pocket. Our data demonstrate the important roles of both TPR and post-SET domains in the histone lysine methyltransferase (HKMT) activity of Smyd3, and show that the hydroxyl group of Tyr239 is critical for the enzymatic activity. The characteristic MYND domain is located nearby to the substrate binding pocket and exhibits a largely positively charged surface. Further biochemical assays show that DNA binding of Smyd3 can stimulate its HKMT activity and the process may be mediated via the MYND domain through direct DNA binding.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.