ArticleLife (Basel, Switzerland)2021
Functional Effects In Silico Prediction for Androgen Receptor Ligand-Binding Domain Novel I836S Mutation.
Article in Life (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 14 citations in OpenAlex.
- Integrated ADME, metabolomics, and multi-target docking of Novel methoxy- and thiophene-substituted benzodioxane hydrazones.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Synthesis and characterization of indole-3-butyric acid-based hydrazones: from multifunctional enzyme inhibition to therapeutic potential for drug development.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Androgen receptor mutations in familial androgen insensitivity syndrome: A metabolic reprogramming pathway to type 2 diabetes susceptibility.World journal of diabetes · 2025Review
- Therapeutic exploration potential of adenosine receptor antagonists through pharmacophore ligand-based modelling and pharmacokinetics studies against Parkinson disease.In silico pharmacology · 2025Article
- 4-(Azolyl)-Benzamidines as a Novel Chemotype for ASIC1a Inhibitors.International journal of molecular sciences · 2024Article
- Four novel mutations in the androgen receptor gene from Vietnamese patients with androgen insensitivity syndrome.Genes & genomics · 2023Article
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Authors and funding
7 authors at 2 institutions in 3 countries.
Funding
Abstract
Over 1000 mutations are described in the androgen receptor (AR) gene. Of those, about 600 were found in androgen insensitivity syndrome (AIS) patients, among which 400 mutations affect the ligand-binding domain (LBD) of the AR protein. Recently, we reported a novel missense mutation c.2507T>G I836S (ClinVarID: 974911) in a patient with complete AIS (CAIS) phenotype. In the present study, we applied a set of computational approaches for the structural analysis of the ligand-binding domains in a wild-type and mutant AR to evaluate the functional impact of the novel I836S mutation. We revealed that the novel I836S substitution leads to a shorter existence time of the ligand's gating tunnel and internal cavity, occurring only in the presence of S836 phosphorylation. Additionally, the analysis of phosphorylation of the 836 mutant residues explained the negative impact on AR homodimerization, since monomer surface changes indirectly impacted the binding site. Our analyses provide evidence that I836S causes disruptions of AR protein functionality and development of CAIS clinical features in patients.
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