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Letter |
Architecture of the TRPM2 channel and its activation mechanism by ADP-ribose and calcium
Structures of the transient receptor potential melastatin 2 channel in the apo resting (closed) state and in the ADP-ribose/Ca2+-bound active (open) state are determined by cryo-electron microscopy.
- Yihe Huang
- , Paige A. Winkler
- & Juan Du
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Article |
Electron cryo-microscopy structure of a human TRPM4 channel
The structure of the Ca2+-activated, non-selective ion channel TRPM4 bound to the agonist Ca2+ and a modulator decavanadate, solved using electron cryo-microscopy.
- Paige A. Winkler
- , Yihe Huang
- & Wei Lü
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Letter |
Cryo-electron microscopy structure of the lysosomal calcium-permeable channel TRPML3
A cryo-electron microscopy structure shows that the mucolipin domain of the lysosomal calcium channel TRPML3 binds phosphatidylinositol-3,5-bisphosphate and gates the channel.
- Marscha Hirschi
- , Mark A. Herzik Jr
- & Seok-Yong Lee
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Letter |
Electron cryo-microscopy structure of the mechanotransduction channel NOMPC
Single-particle electron cryo-microscopy analysis of the mechanotransduction channel NOMPC reveals that it contains a bundle of four helical spring-shaped ankyrin repeat domains that undergo motion, potentially allowing mechanical movement of the cytoskeleton to be coupled to the opening of the channel.
- Peng Jin
- , David Bulkley
- & Yifan Cheng
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Article |
Crystal structure of the epithelial calcium channel TRPV6
The X-ray crystal structure of rat transient receptor potential channel TRPV6 at 3.25 Å resolution is reported, providing new insights into its assembly and calcium-selective permeation.
- Kei Saotome
- , Appu K. Singh
- & Alexander I. Sobolevsky
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Article |
TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action
Cryo-electron microscopy has undergone a resolution revolution—here, this method has been combined with lipid nanodisc technology to solve structures of TRPV1, the receptor for capsaicin, in a membrane bilayer, revealing mechanisms of lipid and ligand regulation.
- Yuan Gao
- , Erhu Cao
- & Yifan Cheng
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Article |
Structure of the TRPA1 ion channel suggests regulatory mechanisms
The high-resolution electron cryo-microscopy structure of the full-length human TRPA1 ion channel is presented; the structure reveals a unique ankyrin repeat domain arrangement, a tetrameric coiled-coil in the centre of the channel that acts as a binding site for inositol hexakisphosphate, an outer poor domain with two pore helices, and a new drug binding site, findings that collectively provide mechanistic insight into TRPA1 regulation.
- Candice E. Paulsen
- , Jean-Paul Armache
- & David Julius
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Article |
TRPV1 structures in distinct conformations reveal activation mechanisms
Using a peptide toxin and small vanilloid agonists as pharmacological probes, high-resolution electron cryo-microscopy structures of rat TRPV1–ligand complexes are solved; these structures highlight conformational differences between TRP and voltage-gated ion channels in their active states, and suggest a dual gating mechanism that may account for the ability of members of the TRP channel superfamily to integrate diverse physiological signals.
- Erhu Cao
- , Maofu Liao
- & David Julius
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Article |
Structure of the TRPV1 ion channel determined by electron cryo-microscopy
A high-resolution electron cryo-microscopy structure of the rat transient receptor potential (TRP) channel TRPV1 in its ‘closed’ state is presented; the overall structure of this ion channel is found to share some common features with voltage-gated ion channels, although several unique, TRP-specific features are also characterized.
- Maofu Liao
- , Erhu Cao
- & Yifan Cheng
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Letter |
Ganglion-specific splicing of TRPV1 underlies infrared sensation in vampire bats
- Elena O. Gracheva
- , Julio F. Cordero-Morales
- & David Julius
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Letter |
Analysis of Drosophila TRPA1 reveals an ancient origin for human chemical nociception
Reactive electrophiles are noxious chemicals, such as acrolein in cigarette smoke, and are detected by the ion channel TRPA1 in humans. Here it is shown that TRPA1 channels sense these chemicals in the gustatory chemosensory neurons of fruitflies and mosquitoes, too. Further findings show that, unlike with other chemical senses such as smell or taste, the detection of reactive electrophiles relies on an ancient sensor that has been conserved in molecular detail through some 500 million years of evolution.
- Kyeongjin Kang
- , Stefan R. Pulver
- & Paul A. Garrity