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Related Experiment Video

Updated: Sep 22, 2025

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

Vanilloid-dependent TRPV1 opening trajectory from cryoEM ensemble analysis.

Do Hoon Kwon¹, Feng Zhang¹, Justin G Fedor¹

¹Department of Biochemistry, Duke University School of Medicine, Durham, NC, 27710, USA.

Nature Communications

|May 24, 2022

Summary

Researchers used cryo-EM to map the conformational changes of the TRPV1 channel upon binding resiniferatoxin (RTx). This reveals a stepwise opening mechanism, offering insights into pain relief mechanisms.

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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

Area of Science:

Structural biology
Biophysics
Molecular pharmacology

Background:

Single particle cryo-electron microscopy (cryo-EM) can capture multiple protein conformations.
Determining the temporal sequence of these conformations in a dynamic process is challenging.
The vanilloid receptor TRPV1 is a key target for pain relief.

Purpose of the Study:

To investigate the temporal resolution of TRPV1 conformational changes upon binding resiniferatoxin (RTx).
To elucidate the step-by-step mechanism of RTx-induced TRPV1 activation.

Main Methods:

Combined thermal titration with single particle cryo-EM.
Analyzed cryo-EM data using ensemble analysis to resolve conformational states.
Investigated the structural dynamics of TRPV1.

Main Results:

RTx binding to TRPV1 initiates a conformational wave.
The sequence of events includes intracellular gate opening, followed by selectivity filter dilation, and pore loop rearrangement.
These changes occur in a stepwise, additive manner across multiple subdomains.

Conclusions:

The study provides a temporal model for RTx-induced TRPV1 activation.
Understanding this mechanism enhances the therapeutic potential of RTx for pain management.
Long-range allostery in TRPV1 is modulated by RTx binding.