Evidence map›Paper›PMID 32572252›Full record

ArticleNature structural & molecular biology2020

Gating of human TRPV3 in a lipid bilayer.

Zengqin Deng, Grigory Maksaev, Michael Rau, Zili Xie, Hongzhen Hu, James A J Fitzpatrick, Peng Yuan

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.3field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

56 citing papers in PubMed, 79 citations in OpenAlex.

  1. An Extracellular Pore‑Targeting Peptide Defines a Designable Allosteric Site in TRPV2.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  13. Structural insights into TRPV2 modulation by probenecid.Nature structural & molecular biology · 2025
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  18. Protein dynamics underlies strong temperature dependence of heat receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Zengqin Deng *Department of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, USA.ORCID http://orcid.org/0000-0002-5658-2068
Grigory Maksaev *Department of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, USA.ORCID http://orcid.org/0000-0001-6242-1634
Michael RauWashington University Center for Cellular Imaging, Washington University School of Medicine, Saint Louis, MO, USA.ORCID http://orcid.org/0000-0001-5170-2000
Zili XieDepartment of Anesthesiology, Washington University School of Medicine, Saint Louis, MO, USA.
Hongzhen HuDepartment of Anesthesiology, Washington University School of Medicine, Saint Louis, MO, USA.
James A J FitzpatrickDepartment of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, USA.ORCID http://orcid.org/0000-0002-7907-3602
Peng YuanDepartment of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, USA. yuanp@wustl.edu.ORCID http://orcid.org/0000-0002-5660-225X
Washington University in St. Louis · US

Funding

TARGETING THE TRANSIENT RECEPTOR POTENTIAL CHANNELS TO IMPROVE BOWEL DYSFUNCTIONR01DK103901 · NIDDK · WASHINGTON UNIVERSITY · PI HU, HONGZHEN · 2015 to 2023
$3.4M
MECHANISMS OF TRPV4-MEDIATED NEUROPATHIC PAINR01AA027065 · NIAAA · WASHINGTON UNIVERSITY · PI HU, HONGZHEN · 2018 to 2022
$2.5M
STRUCTURE AND MECHANISM OF A POLYMODAL TRP ION CHANNELR01NS099341 · NINDS · WASHINGTON UNIVERSITY · PI YUAN, PENG · 2017 to 2021
$1.7M
NIAAA NIH HHS R01 AA027065NIDDK NIH HHS R01 DK103901NINDS NIH HHS R01 NS099341
6 · The paper itself

Abstract

The transient receptor potential cation channel subfamily V member 3 (TRPV3) channel plays a critical role in skin physiology, and mutations in TRPV3 result in the development of a congenital skin disorder, Olmsted syndrome. Here we describe multiple cryo-electron microscopy structures of human TRPV3 reconstituted into lipid nanodiscs, representing distinct functional states during the gating cycle. The ligand-free, closed conformation reveals well-ordered lipids interacting with the channel and two physical constrictions along the ion-conduction pore involving both the extracellular selectivity filter and intracellular helix bundle crossing. Both the selectivity filter and bundle crossing expand upon activation, accompanied by substantial structural rearrangements at the cytoplasmic intersubunit interface. Transition to the inactivated state involves a secondary structure change of the pore-lining helix, which contains a π-helical segment in the closed and open conformations, but becomes entirely α-helical upon inactivation. Together with electrophysiological characterization, structures of TRPV3 in a lipid membrane environment provide unique insights into channel activation and inactivation mechanisms.

Indexed as

Cryoelectron MicroscopyIon Channel GatingLipid BilayersModels, MolecularMutationNanostructuresProtein ConformationTRPV Cation ChannelsLipid BilayersTRPV3 protein, humanTRPV Cation Channels

Identifiers

PMID32572252
PMCPMC7354234
OpenAlexW3035806878

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

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.