ArticleMolecules (Basel, Switzerland)2022
Structural Modeling of TRPA1 Ion Channel-Determination of the Binding Site for Antagonists.
Article in Molecules (Basel, Switzerland), 2022. 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Regulation of transient receptor potential ankyrin 1 by traditional Chinese medicine drugs and their active ingredients.Frontiers in pharmacology · 2025Review
- Bhopal, Dunsmuir and TRPA1: what they have taught us about nociception.Frontiers in allergy · 2025Review
- TRPA1 Inhibition Effects by 3-Phenylcoumarin Derivatives.ACS medicinal chemistry letters · 2024Article
- TRPA1, TRPV1, and Caffeine: Pain and Analgesia.International journal of molecular sciences · 2024Review
- Article
- Dual role of transient receptor potential ankyrin 1 in respiratory and gastrointestinal physiology: From molecular mechanisms to therapeutic targets.Frontiers in physiology · 2024Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
TRPA1 is a transmembrane cation channel, one of the most promising targets in the context of respiratory diseases. Its general structure has already been experimentally resolved, but the binding site of TRPA1 antagonists such as HC-030031, a model methylxanthine derivative, remains unknown. The present study aimed to determine the potential binding site of xanthine antagonists and to describe their binding mode, using a molecular modeling approach. This study represents the first attempt to bring together site-directed mutagenesis reports and the latest cryo-EM structure of an antagonist bound to TRPA1. Our research suggests that the core moiety of HC-030031 binds to a pocket formed by the TRP-like domain and the pre-S1, S4, S5 helices of one subunit. The structure, determined by cryo-EM, shows interactions of a core hypoxanthine moiety in the same area of the binding site, sharing the interaction of xanthine/hypoxanthine with Trp-711. Moreover, the predicted binding mode of HC-030031 assumes interaction with Asn-855, a residue demonstrated to be important for HC-030031 recognition in site-directed mutagenesis studies. Our model proved to be advantageous in a retrospective virtual screening benchmark; therefore, it will be useful in research on new TRPA1 antagonists among xanthine derivatives and their bioisosteres.
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