Tudor Domain Screening Service

Tudor domains are critical epigenetic reader modules that specifically recognize methylated arginine and lysine residues on histones and other proteins, playing essential roles in RNA processing, DNA damage repair, and transcriptional regulation. Their dysfunction is implicated in neurological disorders, cancer, and infertility. CD BioSciences provides expert Tudor domain screening services to accelerate the development of chemical tools and therapeutic leads for these multifaceted targets.

Introduction to Tudor Domain

The Tudor domain is a conserved β-barrel structural module that functions as a versatile reader of methylated post-translational modifications, with specificity for both methylated arginine (e.g., symmetric/asymmetric dimethylarginine) and methylated lysine residues. These domains are integral components of diverse cellular machineries: they mediate spliceosome assembly (e.g., SMN protein), orchestrate the DNA damage response (e.g., 53BP1), regulate chromatin through association with histone demethylases (e.g., JMJD2A), and are essential for germ cell development via piRNA pathway proteins (e.g., TDRD family). Given their central roles in fundamental processes and direct links to diseases—such as spinal muscular atrophy (SMN), cancer (53BP1 dysregulation), and reproductive disorders—Tudor domains represent high-value yet challenging targets. Systematic screening for selective Tudor domain modulators is therefore crucial both for deciphering their complex biology and for developing novel therapeutic strategies across multiple disease areas.

Fig.1 A schematic diagram of the structure of the Tudor domains in the study. (Kawale A A, Burmann B M., 2021)

Our Services

CD BioSciences delivers end-to-end Tudor domain screening solutions designed to address the unique binding preferences and biological contexts of these readers. Our platform combines tailored assay development, sensitive detection technologies, and in-depth data analysis to provide reliable support for your chemical probe development, mechanistic studies, and early-stage drug discovery programs.

Customized Solution for Tudor Domain Screening

At CD BioSciences, we provide fully tailored screening solutions for Tudor domain targets, addressing their unique specificity for methylated arginine and lysine residues. Our approach leverages sensitive, domain-specific assays and flexible screening strategies to deliver precise data for inhibitor discovery, selectivity profiling, and functional validation across diverse biological contexts.

Target Coverage

1. Spliceosomal Tudor Domains: Survival of motor neuron (SMN) protein, SPF30
2. DNA Damage Repair Readers: 53BP1, TDRD3
3. Chromatin & Transcription Regulators: JMJD2A (KDM4A), PHF1 Tudor domain
4. Germ Cell-Specific Readers: TDRD1, TDRD6, TDRD9, TDRKH
5. Custom Targets: Client-provided Tudor domains or engineered variants

Featured Analytical Services

1. Primary Screening & Dose-Response Validation: Identify initial hits through high-throughput screening and confirm their potency with accurate IC₅₀ determination.
2. Methylation-State & Residue Specificity Profiling: Characterize compound selectivity for different methylation states (e.g., arginine vs. lysine, symmetric vs. asymmetric dimethylation).
3. Selectivity Screening: Profile confirmed hits across Tudor family members and other epigenetic readers to ensure target specificity.
4. Structure-Activity Relationship (SAR) Analysis: Guide hit-to-lead optimization using insights from structural data on Tudor domain-ligand interactions.

Cutting-edge Technology Support

Our screening solutions are built upon a foundation of advanced and validated technology platforms, specifically selected and optimized to address the unique challenges of studying Tudor domain interactions. This ensures the generation of high-quality, reliable, and physiologically relevant data.

Workflow of Tudor Domain Screening Service

Application Scenarios

1. Neurological Disease Research: Screening for SMN Tudor domain modulators to investigate therapeutic strategies for spinal muscular atrophy (SMA).
2. Oncology & DNA Repair Targeting: Discovering 53BP1 Tudor inhibitors to modulate DNA damage response and sensitize cancer cells to genotoxic therapies.
3. Chemical Probe Development: Creating selective Tudor domain probes for studying chromatin biology, RNA splicing, and the piRNA pathway.
4. Reproductive Biology & Fertility Research: Identifying modulators of germ cell-specific Tudor proteins (e.g., TDRD family) for developmental and infertility studies.

Our Advantages

1. Comprehensive Target Coverage: We support screening for a wide range of Tudor domain proteins, including those involved in splicing (SMN, SPF30), DNA repair (53BP1, TDRD3), histone demethylation (JMJD2A), and germ cell-specific pathways (TDRD1, TDRD9).
2. Specialized Technology Platform: Our platform employs highly specific detection methods, such as TR-FRET and AlphaScreen assays using methylated peptide/RNA probes, integrated with SPR/MST for detailed binding mode and kinetic analysis.
3. Customized Service Portfolio: We offer tailored analytical services including arginine/lysine methylation-state selectivity analysis, RNA-binding dependency testing, fragment library screening, and functional cellular validation.
4. Cross-Species Application Support: Our services extend across multiple species, supporting Tudor domain screening for human, mouse, and model organisms (e.g., Drosophila, C. elegans).

In addition to Tudor domain screening, CD BioSciences offers a complete portfolio of epigenetic reader screening services. This includes comprehensive screening for bromodomains, chromodomains, MBT domains, PHD fingers, and SRA domains, as well as integrated multiple domains screening. Our fully customizable platform is engineered to support the full scope of your research objectives in epigenetics and RNA biology. Contact us to learn how we can tailor our services to your specific needs.

Reference

1. Kawale A A, Burmann B M. Inherent backbone dynamics fine-tune the functional plasticity of Tudor domains[J]. Structure, 2021, 29(11): 1253-1265. e4.