ArticleNature communications2021
Extracellular cap domain is an essential component of the TRPV1 gating mechanism.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 84 citations in OpenAlex.
- Identification of a human mitochondrial isoform of TRPV1: a thermostat regulating mitochondrial maximal temperature?Cellular and molecular life sciences : CMLS · 2026Article
- Design, synthesis and structural mechanism of action of TRPV1 agonist MSP20 with long-lasting analgesic effect.Nature communications · 2026Article
- Structural diversity of heat-sensing channel TRPV3 with Olmsted syndrome mutations.Nature communications · 2026Article
- TRPV1 antagonism occurs through diverse structural mechanisms.bioRxiv : the preprint server for biology · 2026Article
- CATSPERε extracellular domains are essential for sperm calcium channel assembly and activity modulation.Science advances · 2026Article
- Review
- In silico analysis of sodium ion permeation mechanisms in transient receptor potential vanilloid 1.Scientific reports · 2025Article
- Article
- CATSPERε extracellular domains are essential for sperm calcium channel assembly and activity modulation.bioRxiv : the preprint server for biology · 2025Article
- Structural insights into TRPV2 modulation by probenecid.Nature structural & molecular biology · 2025Article
- Single-crystal structure of the spicy capsaicin.Acta crystallographica. Section C, Structural chemistry · 2025Article
- Plant essential oil targets TRPV3 for skin renewal and structural mechanism of action.Nature communications · 2025Article
- Forty sites of TRP channel regulation.Current opinion in chemical biology · 2025Review
- Insights into Molecular Interactions and Biological Effect of Natural Stilbenoids at the TRPA1 Ion Channel.ChemMedChem · 2025Article
- Missense variant analysis in the TRPV1 ARD reveals the unexpected functional significance of a methionine.PloS one · 2025Article
- Structure- and Ligand-Based Virtual Screening for Identification of Novel TRPV4 Antagonists.Molecules (Basel, Switzerland) · 2024Article
- Identification and development of TRPM4 antagonists to counteract neuronal excitotoxicity.iScience · 2024Article
- Fluorescence labeling strategies for cell surface expression of TRPV1.The Journal of general physiology · 2024Article
- Fluorescence labeling strategies for the study of ion channel and receptor cell surface expression: A comprehensive toolkit for extracellular labeling of TRPV1.bioRxiv : the preprint server for biology · 2024Article
- Dynamic molecular portraits of ion-conducting pores characterize functional states of TRPV channels.Communications chemistry · 2024Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Transient receptor potential (TRP) channels are polymodal molecular sensors involved in numerous physiological processes and implicated in a variety of human diseases. Several structures of the founding member of the TRP channel family, TRPV1, are available, all of which were determined for the protein missing the N- and C-termini and the extracellular S5-P-loop. Here, we present structures of the full-length thirteen-lined ground squirrel TRPV1 solved by cryo-EM. Our structures resolve the extracellular cap domain formed by the S5-P-loops and the C-terminus that wraps around the three-stranded β-sheet connecting elements of the TRPV1 intracellular skirt. The cap domain forms a dome above the pore's extracellular entrance, with four portals leading to the ion conductance pathway. Deletion of the cap increases the TRPV1 average conductance, reduces the open probability and affects ion selectivity. Our data show that both the termini and the cap domain are critical determinants of TRPV1 function.
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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.