GO:0017162 obsolete aryl hydrocarbon receptor binding: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0017162 is an obsolete molecular function term that formerly described binding to an aryl hydrocarbon receptor (AhR).
• The term was retired because 'aryl hydrocarbon receptor binding' is a receptor-ligand interaction better captured by parent terms such as protein binding or signaling receptor binding.
• AhR is a ligand-activated transcription factor that mediates responses to xenobiotics and endogenous ligands, and its binding interactions are central to toxicology and drug safety assessment.
• In silico prediction of drug toxicity often models AhR binding as a key endpoint, illustrating why the concept remains practically important even though the GO term is obsolete.
• Researchers should now annotate AhR interactions using current GO terms and verify binding experimentally rather than relying on the obsolete identifier.
• CRISPR-based models (knockout, point mutation, knock-in, overexpression) enable causal testing of AhR-binding hypotheses in relevant cell types.
Description
GO:0017162, obsolete aryl hydrocarbon receptor binding, is a retired molecular function term in the Gene Ontology that was previously used to annotate proteins capable of binding to an aryl hydrocarbon receptor (AhR). The term belongs to the molecular_function aspect and carried the definition 'Binding to an aryl hydrocarbon receptor,' but it is no longer recommended for annotation because the concept is better represented by more general and stable GO terms. Understanding this obsolete term is useful for researchers who encounter legacy annotations, older datasets, or literature that predates the ontology revision, and who need to map those annotations to current vocabularies. The aryl hydrocarbon receptor is a ligand-activated transcription factor that responds to a wide range of environmental and endogenous chemicals, and its binding interactions are a major focus in toxicology, pharmacology, and drug safety assessment. Computational and in silico approaches frequently attempt to predict whether a compound will bind AhR as part of toxicity screening, which explains why the biological concept behind GO:0017162 remains practically relevant even though the term itself is obsolete. For modern research, the key message is that AhR-binding claims should be supported by experimental evidence and annotated with current GO terms rather than the retired identifier. This article explains what GO:0017162 originally meant, why it was obsoleted, which genes and proteins are involved in AhR biology, and how CRISPR-based models and functional genomics methods can be used to study AhR-binding mechanisms rigorously.
obsolete aryl hydrocarbon receptor binding At A Glance
| GO ID | GO:0017162 |
|---|---|
| GO term | obsolete aryl hydrocarbon receptor binding |
| Ontology | molecular_function |
| Synonym | none |
| Definition | OBSOLETE. Binding to an aryl hydrocarbon receptor. |
| Obsolete status | Retired; not for new annotations |
| Major function | Formerly described binding to aryl hydrocarbon receptor (AhR) |
| Recommended replacement | Use current GO terms such as protein binding or signaling receptor binding |
| Relevance | Legacy annotations, toxicology, drug safety, AhR signaling research |
What Is GO:0017162?
In simple terms, GO:0017162 was a label for 'binding to an aryl hydrocarbon receptor.' The QuickGO definition states: OBSOLETE. Binding to an aryl hydrocarbon receptor. This means the term described a molecular function in which a protein or other molecule physically interacts with an aryl hydrocarbon receptor. Because the ontology curators determined that this concept is not a distinct, well-defined molecular function, the term was marked obsolete and should not be used for new annotations. Researchers should instead use appropriate parent terms such as protein binding or signaling receptor binding, depending on the specific interaction being described.
Why Is obsolete aryl hydrocarbon receptor binding Important in Cell Biology?
Although GO:0017162 is obsolete, the biological process it described, binding to the aryl hydrocarbon receptor, remains highly important because AhR is a central mediator of xenobiotic responses and a key consideration in drug toxicity prediction. In silico toxicology models often include AhR binding as an endpoint, and accurate interpretation of legacy annotations is essential for computational biologists and toxicologists who work with historical datasets. Understanding why the term was retired also helps researchers choose correct current GO terms and design experiments that directly test AhR-binding hypotheses.
• AhR binding is a major endpoint in predictive toxicology and drug safety assessment.
• Legacy datasets and publications may still contain annotations to GO:0017162, requiring careful mapping to current terms.
• AhR mediates responses to environmental contaminants such as dioxins, making its binding interactions clinically and environmentally relevant.
• In silico models of drug toxicity frequently attempt to predict AhR binding, highlighting the practical value of the concept.
• Correct annotation practices prevent misinterpretation of protein function in genomics and proteomics studies.
• CRISPR-based knockout and knock-in models allow causal testing of AhR-binding mechanisms.
• Understanding AhR interactions supports research in cancer biology, immunology, and metabolism.
• Obsolete term awareness improves data curation quality in bioinformatics pipelines.
• AhR-binding predictions can guide prioritization of compounds for experimental validation.
• Functional validation of AhR interactions remains necessary because computational predictions are not definitive.
Molecular Mechanism of obsolete aryl hydrocarbon receptor binding
Historical definition and scope
In simple terms: This term used to mean 'a protein binds to the aryl hydrocarbon receptor.'
GO:0017162 was defined as binding to an aryl hydrocarbon receptor, placing it in the molecular_function aspect of the Gene Ontology. It was intended to capture physical interactions between a gene product and AhR, but the ontology later determined that this concept did not represent a distinct molecular function suitable for annotation. As a result, the term is now obsolete and should not be used in new annotations.
Why the term was obsoleted
In simple terms: The term was retired because 'binding to a receptor' is too generic to be a useful standalone function.
Ontology curation principles favor terms that describe specific, mechanistically informative functions. Binding to a receptor is a broad interaction that is better represented by parent terms such as protein binding or signaling receptor binding, depending on context. The obsoletion of GO:0017162 reflects this curation decision and directs annotators to more appropriate terms.
Aryl hydrocarbon receptor biology
In simple terms: AhR is a receptor that responds to many chemicals and turns genes on or off.
The aryl hydrocarbon receptor is a ligand-activated transcription factor that mediates cellular responses to a variety of xenobiotic and endogenous compounds. Its activation leads to changes in gene expression that can affect drug metabolism, immune function, and cell proliferation. Binding interactions with AhR are therefore central to understanding both normal physiology and toxicological responses.
In silico prediction of AhR binding
In simple terms: Computers are used to guess whether a chemical will bind AhR.
In silico toxicology approaches attempt to predict drug toxicity by modeling interactions such as AhR binding. These computational models are used to prioritize compounds for further testing, but their predictions require experimental validation because they are not definitive. The obsolete GO term is sometimes encountered in legacy datasets that were used to train or benchmark such models.
Experimental validation of AhR binding
In simple terms: Lab experiments are needed to confirm whether a protein really binds AhR.
Direct biochemical methods such as co-immunoprecipitation, pull-down assays, and surface plasmon resonance can test whether a candidate protein interacts with AhR. Functional assays that measure AhR-dependent transcriptional activity provide additional evidence of biologically relevant binding. CRISPR-based genetic models can be used to test the consequences of disrupting candidate binding partners.
Annotation best practices after obsoletion
In simple terms: Use current GO terms instead of the retired one.
Researchers and curators should replace annotations to GO:0017162 with appropriate current terms, such as protein binding or signaling receptor binding, based on the specific interaction being described. When reporting AhR-binding findings, it is good practice to cite the experimental evidence and use stable, non-obsolete GO identifiers. This ensures that datasets remain interoperable and interpretable in modern bioinformatics analyses.
Key Genes Involved in GO:0017162 obsolete aryl hydrocarbon receptor binding
The following genes and proteins are relevant to aryl hydrocarbon receptor biology and to the interpretation of the obsolete GO:0017162 term, based on published literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| AHR | Aryl hydrocarbon receptor; ligand-activated transcription factor | Central to xenobiotic response and drug toxicity prediction |
| ARNT | Aryl hydrocarbon receptor nuclear translocator; forms heterodimer with AhR | Required for AhR-mediated transcriptional activation |
| CYP1A1 | Cytochrome P450 enzyme induced by AhR activation | Biomarker of AhR pathway activity |
| CYP1A2 | Cytochrome P450 enzyme involved in drug metabolism | AhR-regulated; relevant to drug-drug interactions |
| CYP1B1 | Cytochrome P450 enzyme induced by AhR | Associated with xenobiotic metabolism and cancer |
| AHRR | Aryl hydrocarbon receptor repressor | Negative regulator of AhR signaling |
| HSP90AA1 | Heat shock protein 90; chaperone for AhR | Maintains AhR in a ligand-responsive state |
| AIP | Aryl hydrocarbon receptor interacting protein | Modulates AhR stability and function |
| PTGES3 | Prostaglandin E synthase 3; co-chaperone | Part of the AhR chaperone complex |
| NR2F1 | Nuclear receptor; may interact with AhR pathway | Potential crosstalk with AhR signaling |
| NFE2L2 | Nrf2; oxidative stress response transcription factor | Crosstalk with AhR in stress responses |
| RELA | NF-kB subunit; inflammatory signaling | Interacts with AhR in immune regulation |
| TP53 | Tumor suppressor; cellular stress response | Crosstalk with AhR in cancer biology |
| ESR1 | Estrogen receptor alpha | Potential crosstalk with AhR signaling |
| MYC | Oncogene; cell proliferation | AhR influences MYC expression in some contexts |
| IL6 | Interleukin 6; inflammatory cytokine | AhR modulates inflammatory cytokine expression |
| TGFB1 | Transforming growth factor beta 1 | AhR influences TGF-beta signaling |
How Is obsolete aryl hydrocarbon receptor binding Regulated?
The aryl hydrocarbon receptor pathway is regulated at multiple levels, including ligand availability, chaperone-mediated stabilization, and feedback repression. In silico models of drug toxicity often incorporate AhR binding as a regulated endpoint, reflecting the pathway's sensitivity to chemical exposure. Because GO:0017162 is obsolete, modern studies should describe AhR regulation using current GO terms and experimental evidence.
obsolete aryl hydrocarbon receptor binding and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| AHR | Toxicology, cancer, immune regulation | AHR knockout cell lines |
| CYP1A1 | Xenobiotic metabolism, cancer biomarker | CYP1A1 reporter cell line |
| AHRR | Feedback regulation of AhR signaling | AHRR overexpression model |
| ARNT | AhR transcriptional activity | ARNT knockout model |
| HSP90AA1 | AhR stability and function | HSP90AA1 point mutation model |
Aryl hydrocarbon receptor binding in toxicology and drug safety
AhR binding is a key consideration in predictive toxicology because activation of AhR by xenobiotics can lead to adverse effects. In silico models attempt to predict drug toxicity by evaluating AhR binding, but these predictions must be validated experimentally. The obsolete GO term GO:0017162 may appear in legacy datasets used for such modeling, so researchers should map it to current terms.
AhR signaling in cancer
AhR signaling has been implicated in cancer biology, where it can influence cell proliferation, differentiation, and survival. Binding interactions with AhR are therefore of interest for understanding tumor-promoting or tumor-suppressive mechanisms. CRISPR-based models can help determine whether specific AhR-binding partners are causally involved in cancer phenotypes.
AhR and immune regulation
AhR is involved in immune regulation, including effects on inflammatory cytokine expression and immune cell differentiation. Binding to AhR by endogenous or exogenous ligands can modulate these responses. Experimental models that disrupt AhR or its binding partners can clarify the role of these interactions in immune-related diseases.
Legacy annotations and data interpretation
The obsoletion of GO:0017162 means that older datasets may contain annotations that are no longer valid. Researchers analyzing such data should be aware that 'aryl hydrocarbon receptor binding' annotations may need to be reinterpreted using current GO terms. This is particularly important in computational toxicology, where legacy data are often reused.
From obsolete aryl hydrocarbon receptor binding-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does AHR loss affect xenobiotic response? | AHR knockout cell line |
| Does a specific AHR mutation alter ligand binding? | AHR point mutation knock-in |
| Can a candidate binding partner be tagged for interaction studies? | Tagged knock-in of candidate gene |
| Does overexpression of AHRR repress AhR signaling? | AHRR overexpression cell line |
| Is ARNT required for AhR-mediated transcription? | ARNT knockout cell line |
| Does a compound induce CYP1A1 via AhR? | CYP1A1 reporter assay with AHR knockout control |
How to Study the obsolete aryl hydrocarbon receptor binding Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Co-immunoprecipitation | Physical interaction between proteins | Validate AhR binding partners |
| Surface plasmon resonance | Binding affinity and kinetics | Quantify AhR-ligand interactions |
| Reporter gene assay | AhR transcriptional activity | Screen compounds for AhR activation |
| CRISPR knockout | Loss-of-function effects | Test causal role of candidate genes |
| CRISPR knock-in | Tagged or mutant protein expression | Study binding domains in endogenous context |
| RNA-seq | Global gene expression changes | Identify AhR-regulated pathways |
| Proteomics | Protein abundance and interactions | Discover AhR-associated complexes |
| In silico docking | Predicted binding poses | Prioritize compounds for testing |
Biochemical binding assays
Co-immunoprecipitation, pull-down assays, and surface plasmon resonance can directly test whether a protein binds to AhR. These methods provide physical evidence of interaction and can be used to validate computational predictions.
Transcriptional reporter assays
AhR-dependent transcriptional activity can be measured using reporter genes driven by AhR-responsive promoters, such as CYP1A1. These assays link binding events to functional outcomes and are useful for screening compounds.
CRISPR-based functional genomics
CRISPR knockout, point mutation, knock-in, and overexpression models allow causal testing of genes involved in AhR binding and signaling. These models can be combined with transcriptomics or proteomics to dissect pathway mechanisms.
In silico modeling and bioinformatics
Computational approaches predict AhR binding and toxicity, but require experimental validation. Bioinformatics pipelines should map obsolete GO terms like GO:0017162 to current annotations to maintain data quality.
How CRISPR Can Be Used to Study GO:0017162 obsolete aryl hydrocarbon receptor binding
Knockout
CRISPR knockout of AHR or its binding partners can abolish specific interactions and reveal their functional consequences. Knockout models are useful for confirming whether a candidate gene is required for AhR-mediated responses.
Point Mutation
Point mutations can be introduced into AHR or candidate binding partners to disrupt specific interaction interfaces while preserving overall protein structure. These models help distinguish binding-dependent from binding-independent functions.
Knock-in
Tagged knock-in of AHR or interacting proteins enables endogenous labeling for interaction and localization studies. Knock-in models can also express disease-associated variants to test their impact on AhR binding.
Overexpression
Overexpression of AHR, AHRR, or candidate binding partners can amplify or suppress AhR signaling for pathway analysis. These models are useful for screening downstream effects and validating regulatory relationships.
How EDITGENE Supports obsolete aryl hydrocarbon receptor binding Research
Researchers studying obsolete aryl hydrocarbon receptor binding-related genes often need to determine whether a candidate gene is causally involved in AhR signaling or toxicity. EDITGENE provides CRISPR-based cell model services that enable precise genetic perturbations and functional readouts, helping teams move from computational predictions to experimental validation.
Contact EDITGENE today to design your custom CRISPR model for obsolete aryl hydrocarbon receptor binding research.
Frequently Asked Questions About obsolete aryl hydrocarbon receptor binding
What is GO:0017162?
GO:0017162 is an obsolete Gene Ontology molecular function term that formerly described binding to an aryl hydrocarbon receptor.
Why is GO:0017162 obsolete?
It was retired because 'binding to a receptor' is a broad interaction better represented by current terms such as protein binding or signaling receptor binding.
What genes are involved in aryl hydrocarbon receptor binding?
Key genes include AHR, ARNT, AHRR, HSP90AA1, AIP, and CYP1A1, among others.
What is the aryl hydrocarbon receptor?
AhR is a ligand-activated transcription factor that mediates responses to xenobiotics and endogenous compounds.
How can I study AhR binding experimentally?
Biochemical assays such as co-immunoprecipitation and surface plasmon resonance, combined with CRISPR models, can test AhR binding.
What GO term should I use instead of GO:0017162?
Use current terms such as protein binding or signaling receptor binding, depending on the specific interaction.
Is AhR binding important for drug safety?
Yes, AhR binding is a key endpoint in predictive toxicology and drug safety assessment.
Can CRISPR help study AhR binding?
Yes, CRISPR knockout, point mutation, knock-in, and overexpression models enable causal testing of AhR-binding hypotheses.
What diseases are linked to AhR signaling?
AhR signaling has been implicated in toxicology, cancer, and immune regulation.
How do I interpret legacy annotations to GO:0017162?
Legacy annotations should be mapped to current GO terms and validated experimentally before reuse.
Conclusion
GO:0017162 obsolete aryl hydrocarbon receptor binding is a retired molecular function term that once described binding to the aryl hydrocarbon receptor. Although it is no longer used for annotation, the underlying biology remains important in toxicology, drug safety, cancer, and immunology. Researchers should use current GO terms and experimental validation, including CRISPR-based models, to study AhR interactions rigorously.
References
- 1. Vedani A et al.. 2006. The challenge of predicting drug toxicity in silico.. Basic Clin Pharmacol Toxicol 99(3):195-208 PMID: 16930291